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General Information
Symbol
Dmel\ph-p
Species
D. melanogaster
Name
polyhomeotic proximal
Annotation Symbol
CG18412
Feature Type
FlyBase ID
FBgn0004861
Gene Model Status
Stock Availability
Gene Snapshot
polyhomeotic proximal (ph-p) encodes a stoichiometric subunit of the Polycomb repressive complex 1. The complex silences a variety of genes involved in developmental patterning, regulation of cell proliferation, differentiation and polarity. Together with its paralog ph-d, ph-p functions as a tumor suppressor gene. [Date last reviewed: 2019-03-14]
Also Known As
ph, Polyhomeotic, EG:87B1.5 , PHP, ph-proximal
Key Links
Genomic Location
Cytogenetic map
Sequence location
X:2,126,210..2,138,371 [-]
Recombination map
1-0.6
Sequence
Other Genome Views
The following external sites may use different assemblies or annotations than FlyBase.
Function
GO Summary Ribbons
Protein Family (UniProt)
-
Summaries
Gene Group (FlyBase)
POLYCOMB REPRESSIVE COMPLEX 1 (CORE SUBUNITS) -
The Polycomb repressive complex 1 (PRC1) is a Polycomb group complex. It binds to histone H3K27me3 (histone H3 K27 methylation is catalyzed by PRC2) and monoubiquitinates H2A on K119. This leads to chromatin compaction, RNA polymerase II stalling and gene silencing. (Adapted from FBrf0179742 and FBrf0228921).
Protein Function (UniProtKB)
Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. Component of the PcG multiprotein PRC1 complex, a complex that acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-118', rendering chromatin heritably changed in its expressibility. Plays a role in regulating the expression of other pair-rule genes such as eve, ftz, and H.
(UniProt, P39769)
Phenotypic Description (Red Book; Lindsley and Zimm 1992)
ph: polyhomeotic (P. Santamaria)
A member of the Polycomb group of genes; seems to be the only one that is strongly required both maternally and zygotically for normal embryonic development. Two mutagenic events are necessary to produce null mutations, suggesting that the locus is complex, and in fact molecular determinations indicate that the locus comprises a direct repeat. Single-event mutations are viable as males and homozygous females; such mutations produce transformations similar to those of known dominant gain-of-function mutants in the ANTC and BXC, i.e., transformation of wings to halteres, second and third legs to first legs, and anterior abdominal segments to more posterior segments (mutants may also show loss of the humerus). Two-event lethal mutations die in mid embryogenesis and completely lack ventral and abdominal epidermal derivatives; they show transformations of most of the segments toward the eighth abdominal segment (Dura et al., 1988). There is an alteration in the pattern of axon pathways in the CNS. The axons fail to form commissures or connectives but instead form large bundles in the middle of each hemi-ganglion (Smouse et al., 1988). Trans heterozygotes between viable and lethal alleles or between viable alleles and a deficiency for ph die in late embryogenesis and exhibit posteriorly directed transformations; i.e. viable alleles are haplo insufficient. Dura et al. (1987) postulate that mutations can occur in either or both of the repeated sequences such that -+/-+ = +-/+- = -+/+- = viable mutant constitutions (--/++ not stated to be mutant); -+/-- = +-/-- = late embryonic lethals; and --/-- = mid-embryonic-stage lethals. The ph+ product is required autonomously in imaginal cells. A total lack of ph+ function prevents viability of the cuticular derivatives of these cells, but amorphic ph clones induced in late third instar survive. ph has a strong maternal effect on segmental identity and epidermal development that cannot be rescued by a single paternally supplied dose of ph+ in the zygote (Dura et al., 1988). The expression of ph is inversely related to dosage of the ANTC and the BXC; the gene interacts with Pc, Pcl, and esc (Dura et al., 1985). At the shortened germ band stage (but not at the blastoderm stage), ph seems to be involved in the regulation, not only of the homeotic genes Scr and Ubx, but also in the regulation of the segmentation genes ftz, eve, and en (Dura and Ingham, 1988).
Summary (Interactive Fly)
transcription factor - zinc finger - Polycomb group - maintain the repression of in the anterior cells abutting the anterior-posterior boundary of the developing wing
Gene Model and Products
Number of Transcripts
4
Number of Unique Polypeptides
2

Please see the GBrowse view of Dmel\ph-p or the JBrowse view of Dmel\ph-p 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 5.52
Low-frequency RNA-Seq exon junction(s) not annotated.
Annotated transcripts do not represent all supported alternative splices within 5' UTR.
Gene model reviewed during 5.56
Sequence Ontology: Class of Gene
Transcript Data
Annotated Transcripts
Name
FlyBase ID
RefSeq ID
Length (nt)
Assoc. CDS (aa)
FBtr0070432
5940
1589
FBtr0301515
5724
1346
FBtr0343589
5695
1346
FBtr0345598
6048
1346
Additional Transcript Data and Comments
Reported size (kB)
6.4, 6.1 (northern blot)
Comments
External Data
Crossreferences
Polypeptide Data
Annotated Polypeptides
Name
FlyBase ID
Predicted MW (kDa)
Length (aa)
Theoretical pI
RefSeq ID
GenBank
FBpp0070416
167.3
1589
9.55
FBpp0290730
141.2
1346
9.25
FBpp0310186
141.2
1346
9.25
FBpp0311667
141.2
1346
9.25
Polypeptides with Identical Sequences

The group(s) of polypeptides indicated below share identical sequence to each other.

1346 aa isoforms: ph-p-PB, ph-p-PC, ph-p-PD
Additional Polypeptide Data and Comments
Reported size (kDa)
1589 (aa); 170 (kD observed)
1589 (aa); 170 (kD observed); 169 (kD predicted)
Comments
Antibodies specific to ph-p protein were raised.
ph-p protein binds to about 80 sites along the polytene chromosomes that are distributed throughout the genome. The bound sites largely overlap those bound by Pc protein. ph-p binds to insertion sites of constructs containing sequences from the bxd region of Ubx showing that the binding is DNA-sequence dependent.
The sequences of ph-p and ph-d may be aligned along a stretch of 1442 amino acids along which they show great similarity.
External Data
Subunit Structure (UniProtKB)
Component of PRC1 complex, which contains many PcG proteins like Pc, ph, Scm, Psc, Sce and also chromatin-remodeling proteins such as histone deacetylases. This complex is distinct from the Esc/E(z) complex, at least composed of esc, E(z), Su(z)12, Rpd3 and Caf1. The 2 complexes however cooperate and interact together during the first 3 hours of development to establish PcG silencing. Interacts with the SAM domain of Scm via its SAM domain in vitro. Interacts with Trl in vivo and with corto in vitro.
(UniProt, P39769)
Crossreferences
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\ph-p 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 (6 terms)
CV Term
Evidence
References
inferred from direct assay
inferred from direct assay
inferred from physical interaction with FLYBASE:barr; FB:FBgn0014127
inferred from physical interaction with UniProtKB:P41046
(assigned by UniProt )
inferred from physical interaction with UniProtKB:Q9VHA0
(assigned by UniProt )
Terms Based on Predictions or Assertions (1 term)
CV Term
Evidence
References
inferred from electronic annotation with InterPro:IPR012313
(assigned by InterPro )
Biological Process (8 terms)
Terms Based on Experimental Evidence (8 terms)
CV Term
Evidence
References
Terms Based on Predictions or Assertions (0 terms)
Cellular Component (3 terms)
Terms Based on Experimental Evidence (3 terms)
CV Term
Evidence
References
Terms Based on Predictions or Assertions (1 term)
CV Term
Evidence
References
traceable author statement
Expression Data
Expression Summary Ribbons
Colored tiles in ribbon indicate that expression data has been curated by FlyBase for that anatomical location. Colorless tiles indicate that there is no curated data for that location.
For complete stage-specific expression data, view the modENCODE Development RNA-Seq section under High-Throughput Expression below.
Transcript Expression
Polypeptide Expression
immunolocalization
Stage
Tissue/Position (including subcellular localization)
Reference
mitotic domain

Comment: not distinguished from ph-d

Additional Descriptive Data
No differences in staining pattern were observed when assaying for ph-p and ph-d proteins in embryos.
ph protein starts to be detected in embryos in the nuclei at the periphery starting at cell cyle 10 and is clearly observed by cell cycle 11. In the cellular blastoderm stage, it is ubiquitously distributed but is more concentrated at the periphery and in central nuclei. Protein continues to be ubiquitously distributed in the embryo with higher concentrations in certain tissues. From gastrulation on, nuclei of cells that are undergoing mitosis appear to be more heavily stained. Within these putative mitotic domains, individual chromosomes appear to be stained. In stages 10 and 11, expression is periodic in the developing CNS. It is not clear if ph protein is in neuroblasts at stage 11 but it is present in neuroblast derivatives in stage 12 in the neuromeres of all segments. Expression in the nervous system continues throughout embryogenesis. ph protein is found mainly in the cell bodies of CNS neurons and may be present in glial cells. It is observed in the campaniform sensillae of the PNS in late embryos. ph protein is observed in eye-antennal, leg, wing, and haltere discs in third instar larvae. While staining is observed all over the discs, some regions stain more intensely. For example, in eye-antennal discs, regions that will give rise to the posterior part of the eye and the orbital region as well as the proximal part of the antenna on the lateral side stain more intensely. The haltere disc consistantly shows a gradient of expression. The antibody does not distinguish between ph-p protein and ph-d protein.
The distribution of polyhomeotic protein and Pc protein is nearly indistinguishable in embryos.
Marker for
 
Subcellular Localization
CV Term
Evidence
References
Expression Deduced from Reporters
High-Throughput Expression Data
Associated Tools

GBrowse - Visual display of RNA-Seq signals

View Dmel\ph-p in GBrowse 2
RNA-Seq by Region - Search RNA-Seq expression levels by exon or genomic region
Reference
See Gelbart and Emmert, 2013 for analysis details and data files for all genes.
Developmental Proteome: Life Cycle
Developmental Proteome: Embryogenesis
External Data and Images
Linkouts
FLIGHT - Cell culture data for RNAi and other high-throughput technologies
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
Alleles, Insertions, and Transgenic Constructs
Classical and Insertion Alleles ( 38 )
For All Classical and Insertion Alleles Show
 
Other relevant insertions
Transgenic Constructs ( 21 )
For All Alleles Carried on Transgenic Constructs Show
Transgenic constructs containing/affecting coding region of ph-p
Transgenic constructs containing regulatory region of ph-p
Deletions and Duplications ( 24 )
Phenotypes
For more details about a specific phenotype click on the relevant allele symbol.
Lethality
Allele
Other Phenotypes
Allele
Phenotype manifest in
Allele
mesothoracic leg & sex comb | ectopic
mesothoracic leg & sex comb tooth | ectopic
metathoracic leg & sex comb tooth | ectopic
Orthologs
Human Orthologs (via DIOPT v7.1)
Homo sapiens (Human) (9)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
9 of 15
Yes
Yes
8 of 15
No
Yes
7 of 15
No
Yes
1 of 15
No
Yes
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
Model Organism Orthologs (via DIOPT v7.1)
Mus musculus (laboratory mouse) (6)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
8 of 15
Yes
Yes
7 of 15
No
Yes
6 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
Rattus norvegicus (Norway rat) (5)
6 of 13
Yes
Yes
5 of 13
No
Yes
5 of 13
No
Yes
1 of 13
No
No
1 of 13
No
No
Xenopus tropicalis (Western clawed frog) (2)
3 of 12
Yes
Yes
3 of 12
Yes
Yes
Danio rerio (Zebrafish) (11)
9 of 15
Yes
No
9 of 15
Yes
Yes
6 of 15
No
Yes
5 of 15
No
Yes
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
Yes
Caenorhabditis elegans (Nematode, roundworm) (0)
No records found.
Arabidopsis thaliana (thale-cress) (0)
No records found.
Saccharomyces cerevisiae (Brewer's yeast) (0)
No records found.
Schizosaccharomyces pombe (Fission yeast) (1)
1 of 12
Yes
No
Orthologs in Drosophila Species (via OrthoDB v9.1) ( EOG09190BUR )
Organism
Common Name
Gene
AAA Syntenic Ortholog
Multiple Dmel Genes in this Orthologous Group
Drosophila melanogaster
fruit fly
Drosophila melanogaster
fruit fly
Drosophila suzukii
Spotted wing Drosophila
Drosophila suzukii
Spotted wing Drosophila
Drosophila simulans
Drosophila sechellia
Drosophila sechellia
Drosophila sechellia
Drosophila erecta
Drosophila erecta
Drosophila yakuba
Drosophila ananassae
Drosophila ananassae
Drosophila pseudoobscura pseudoobscura
Drosophila pseudoobscura pseudoobscura
Drosophila persimilis
Drosophila persimilis
Drosophila willistoni
Drosophila virilis
Drosophila mojavensis
Drosophila grimshawi
Orthologs in non-Drosophila Dipterans (via OrthoDB v9.1) ( EOG0915022V )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Musca domestica
House fly
Glossina morsitans
Tsetse fly
Lucilia cuprina
Australian sheep blowfly
Mayetiola destructor
Hessian fly
Aedes aegypti
Yellow fever mosquito
Anopheles darlingi
American malaria mosquito
Anopheles gambiae
Malaria mosquito
Culex quinquefasciatus
Southern house mosquito
Orthologs in non-Dipteran Insects (via OrthoDB v9.1) ( EOG090W0JZD )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Bombyx mori
Silkmoth
Apis florea
Little honeybee
Apis mellifera
Western honey bee
Bombus impatiens
Common eastern bumble bee
Bombus terrestris
Buff-tailed bumblebee
Linepithema humile
Argentine ant
Megachile rotundata
Alfalfa leafcutting bee
Nasonia vitripennis
Parasitic wasp
Dendroctonus ponderosae
Mountain pine beetle
Tribolium castaneum
Red flour beetle
Pediculus humanus
Human body louse
Cimex lectularius
Bed bug
Acyrthosiphon pisum
Pea aphid
Acyrthosiphon pisum
Pea aphid
Zootermopsis nevadensis
Nevada dampwood termite
Orthologs in non-Insect Arthropods (via OrthoDB v9.1) ( EOG090X0K5C )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Strigamia maritima
European centipede
Strigamia maritima
European centipede
Ixodes scapularis
Black-legged tick
Stegodyphus mimosarum
African social velvet spider
Stegodyphus mimosarum
African social velvet spider
Tetranychus urticae
Two-spotted spider mite
Tetranychus urticae
Two-spotted spider mite
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Orthologs in non-Arthropod Metazoa (via OrthoDB v9.1) ( None identified )
No non-Arthropod Metazoa orthologies identified
Paralogs
Paralogs (via DIOPT v7.1)
Drosophila melanogaster (Fruit fly) (6)
6 of 10
2 of 10
1 of 10
1 of 10
1 of 10
1 of 10
Human Disease Associations
FlyBase Human Disease Model Reports
Disease Model Summary Ribbon
Disease Ontology (DO) Annotations
Models Based on Experimental Evidence ( 1 )
Allele
Disease
Evidence
References
Potential Models Based on Orthology ( 1 )
Human Ortholog
Disease
Evidence
References
Modifiers Based on Experimental Evidence ( 1 )
Allele
Disease
Interaction
References
Comments on Models/Modifiers Based on Experimental Evidence ( 0 )
 
Disease Associations of Human Orthologs (via DIOPT v7.1 and OMIM)
Note that ortholog calls supported by only 1 or 2 algorithms (DIOPT score < 3) are not shown.
Functional Complementation Data
Functional complementation data is computed by FlyBase using a combination of the orthology data obtained from DIOPT and OrthoDB and the allele-level genetic interaction data curated from the literature.
Interactions
Summary of Physical Interactions
esyN Network Diagram
Show neighbor-neighbor interactions:
Select Layout:
Legend:
Protein
RNA
Selected Interactor(s)
Interactions Browser

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

Please look at the allele data for full details of the genetic interactions
Starting gene(s)
Interaction type
Interacting gene(s)
Reference
Starting gene(s)
Interaction type
Interacting gene(s)
Reference
External Data
Subunit Structure (UniProtKB)
Component of PRC1 complex, which contains many PcG proteins like Pc, ph, Scm, Psc, Sce and also chromatin-remodeling proteins such as histone deacetylases. This complex is distinct from the Esc/E(z) complex, at least composed of esc, E(z), Su(z)12, Rpd3 and Caf1. The 2 complexes however cooperate and interact together during the first 3 hours of development to establish PcG silencing. Interacts with the SAM domain of Scm via its SAM domain in vitro. Interacts with Trl in vivo and with corto in vitro.
(UniProt, P39769 )
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.
MIST (genetic) - An integrated Molecular Interaction Database
MIST (protein-protein) - An integrated Molecular Interaction Database
Pathways
Genomic Location and Detailed Mapping Data
Chromosome (arm)
X
Recombination map
1-0.6
Cytogenetic map
Sequence location
X:2,126,210..2,138,371 [-]
FlyBase Computed Cytological Location
Cytogenetic map
Evidence for location
2D2-2D3
Limits computationally determined from genome sequence between P{EP}ActnEP1193&P{EP}CG4322EP1631 and P{EP}EP1460&P{EP}CG2924EP1596
Experimentally Determined Cytological Location
Cytogenetic map
Notes
References
Experimentally Determined Recombination Data
Location
1-0.5
Left of (cM)
Right of (cM)
Notes
Stocks and Reagents
Stocks (19)
Genomic Clones (6)
 

Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete

cDNA Clones (28)
 

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

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

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

    cDNA Clones, End Sequenced (ESTs)
    BDGP DGC clones
    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: ph-p CG18414
    Source for identity of: ph-p CG18412 CG18414
    Source for database merge of
    Additional comments
    Source for identity of ph-p CG18412 CG18414 was sequence comparison ( date:000425 ).
    "ph-p" may be allelic to "rsc".
    Other Comments
    Pc-G proteins can silence gene expression at a large number of chromosomal locations. Repression is observed even with separation distances of up to 3.0kb between target promoters and binding sites for tethered Pc-G proteins. Silencing depends upon the dosage of endogenous, untethered ph-d/ph-p protein, implying that tethered proteins work by recruiting other Pc-G components.
    Pc, Scm, Psc, ph-p and ph-d contribute to the PRC1 (Polycomb repressive complex 1). PRC1 directly antagonizes ATP-dependent remodeling of nucleosomal arrays in a purified system and may directly modulate (and be modified by) SWI/SNF (brm/mor) activity.
    The C-terminal region of ph-p can self-associate in vitro and this self-association is a function of the SAM domain. Mutational analysis identifies the residues important for oligomerisation.
    ph-p, Psc and Pc proteins coimmunoprecipitate from nuclear extracts. Interacting domains are identified and delimited using the two-hybrid system, the interactions are shown to be direct by using an in vitro binding assay.
    Interactions between en and ph-p are required to maintain the anterior-posterior boundary and posterior cell fate in the wing.
    Normal ph-p expression depends on exd expression in vivo.
    ph-d and ph-p are differentially regulated at the mRNA level during development.
    ph-p and ph-d proteins have different effects on the bxd regulatory region.
    Mutations in the ph-p and ph-d transcription units have differing effects on the regulation of a reporter gene under the control of a bxd regulatory region.
    The SPM domain of ph-p and Scm mediates direct interaction between these proteins, and is sufficient for these protein interactions.
    Psc protein coimmunoprecipitates Pc and ph-d/ph-p indicating they are members of a common multimeric protein complex. These proteins are associated with identical regulatory elements of en in tissue culture cells and differentially distributed on regulatory sequences of inv.
    In an effort to subdivide the Pc-group genes functionally, the phenotypes of adult flies heterozygous for every pairwise combination of Pc-group mutation were examined. Most duplications of Pc-group genes neither exhibit anterior transformations nor suppress the extra sex comb phenotype of Pc-group mutations, suggesting that not all Pc-group genes behave as predicted by the mass action model.
    Early ph-p gene expression is under the control of bcd and en as activators and of osk as an inhibitor. The negative autoregulation of ph-p starts at the blastoderm stage and is partly mediated by a transvection effect. As the number of functional copies of ph-p increases a concomitant reduction of the transcription in each copy is observed. This regulation is ensured positively by the trx group and negatively by the Pc group gene products. An equilibrium between these two states of chromatin activity ensures an accurate level of ph-p transcription.
    ph-d and ph-p activation in germ band elongated embryos could be mediated by en binding to en-binding sites upstream of each of the two polyhomeotic transcription units.
    ph-d and ph-p product is found on larval salivary chromosomes at about 100 specific loci, in the same positions as the products of Pc and Pcl genes.
    P-element transposons bearing ph-p regulatory sequences preferentially insert into regions containing known ph-p and Pc protein binding sites, perhaps because shared regulatory proteins bring transposons and insertion sites into close proximity.
    Sequences from the 5' region of ph-p confer variegation on mini-w and Ecol\lacZ genes in euchromatic contexts. This variegation is sensitive to ph-p and Pc mutations. The ph-p regulatory DNA can also mediate transvection of the mini-w gene, which is abolished in ph-p but not z mutant backgrounds.
    ph-p and ph-d gene products bind polytene chromosomes at 45 locations where other Pc-group proteins, encoded by Pc and Psc, are present.
    There is considerable overlap of chromosomal binding sites for Psc, Su(z)2, z, Pc and the ph-p and ph-d proteins.
    The bithorax complex genes are regulated by the Pc group of genes, including ph-p and ph-d, acting via 'Pc group response elements' (PREs), that can work even when removed from the normal bithorax complex context. The Pc group products apparently provide stable memory or imprinting of boundaries which are specified by gap and pair-rule regulators.
    ph-p protein contains a possible zinc finger motif, a Ser/Thr-rich region and Gln repeats, consistent with a role for ph-p in DNA and protein interactions. ph-p protein binds to about 80 sites on polytene chromosomes and extensive overlap exists between the binding sites of ph-p and Pc on polytene chromosomes.
    Pc and ph-d/ph-p proteins are constituents of a soluble multimeric nuclear protein complex.
    A member of the Polycomb group of genes; seems to be the strongly required both maternally and zygotically for normal embryonic development.
    Two mutagenic events are necessary to produce null mutations, in both ph-d and ph-p. Single-event mutations are viable as males and homozygous females; such mutations produce transformations similar to those of known dominant gain-of-function mutants in the ANTC and BXC, i.e., transformation of wings to halteres, second and third legs to first legs and anterior abdominal segments to more posterior segments (mutants may also show loss of the humerus). Trans heterozygotes between viable and lethal alleles or between viable alleles and a deficiency for ph-d and ph-p die in late embryogenesis and exhibit posteriorly directed transformations; i.e. viable alleles are haplo-insufficient. The ph-d+/ph-p+ product is required autonomously in imaginal cells. A total lack of ph-d+/ph-p+ function prevents viability of the cuticular derivatives of these cells, but amorphic clones induced in late third instar survive.
    Mutations of genes in the polycomb group (esc, E(z), Pc, ph-p, ph-d, Scm, Pcl, Sce, Asx, Psc, pho and Antp) cause abnormal segmental development due to the ectopic expression of abd-A and Abd-B.
    The Pc group genes are negative regulators of homeotic genes and have pleiotropic effects on development.
    At the shortened germ band stage (but not at the blastoderm stage), ph-d/ph-p seems to be involved in the regulation, not only of the homeotic genes Scr and Ubx, but also in the regulation of the segmentation genes ftz, eve and en.
    Two-event lethal mutations die in mid-embryogenesis and completely lack ventral and abdominal epidermal derivatives; they show transformations of most of the segments toward the eighth abdominal segment. ph-d/ph-p has a strong maternal effect on segmental identity and epidermal development that cannot be rescued by a single paternally supplied dose of ph-d+/ph-p+ in the zygote.
    There is an alteration in the pattern of axon pathways in the CNS in ph-d,ph-p mutants. The axons fail to form commissures or connectives but instead form large bundles in the middle of each hemi-ganglion.
    ph-d and ph-p form a complex locus, total elimination of 'polyhomeotic' function requires mutations of both the proximal and distal genes.
    Origin and Etymology
    Discoverer
    Etymology
    Identification
    External Crossreferences and Linkouts ( 63 )
    Sequence Crossreferences
    NCBI Gene - Gene integrates information from a wide range of species. A record may include nomenclature, Reference Sequences (RefSeqs), maps, pathways, variations, phenotypes, and links to genome-, phenotype-, and locus-specific resources worldwide.
    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.
    RefSeq - A comprehensive, integrated, non-redundant, well-annotated set of reference sequences including genomic, transcript, and protein.
    UniProt/Swiss-Prot - Manually annotated and reviewed records of protein sequence and functional information
    UniProt/TrEMBL - Automatically annotated and unreviewed records of protein sequence and functional information
    Other crossreferences
    Drosophila Genomics Resource Center - Drosophila Genomics Resource Center (DGRC) cDNA clones
    Eukaryotic Promoter Database - A collection of databases of experimentally validated promoters for selected model organisms.
    Fly-FISH - A database of Drosophila embryo and larvae mRNA localization patterns
    Flygut - An atlas of the Drosophila adult midgut
    GenomeRNAi - A database for cell-based and in vivo RNAi phenotypes and reagents
    iBeetle-Base - RNAi phenotypes in the red flour beetle (Tribolium castaneum)
    KEGG Genes - Molecular building blocks of life in the genomic space.
    modMine - A data warehouse for the modENCODE project
    PDB - An information portal to biological macromolecular structures
    SignaLink - A signaling pathway resource with multi-layered regulatory networks.
    Linkouts
    BioGRID - A database of protein and genetic interactions.
    DroID - A comprehensive database of gene and protein interactions.
    DRSC - Results frm RNAi screens
    FLIGHT - Cell culture data for RNAi and other high-throughput technologies
    FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
    FlyMine - An integrated database for Drosophila genomics
    Interactive Fly - A cyberspace guide to Drosophila development and metazoan evolution
    InterologFinder - Protein-protein interactions (PPI) from both known and predicted PPI data sets.
    MIST (genetic) - An integrated Molecular Interaction Database
    MIST (protein-protein) - An integrated Molecular Interaction Database
    Synonyms and Secondary IDs (27)
    Reported As
    Symbol Synonym
    ph
    (Simoes da Silva et al., 2017, Sievers et al., 2014, Feng et al., 2012, Gutiérrez et al., 2012, Robinson et al., 2012, Bantignies et al., 2011, Feng et al., 2011, Martinez and Cavalli, 2010, Saj et al., 2010, Bejarano and Milán, 2009, Classen et al., 2009, Fang et al., 2009, Martinez et al., 2009, Moazzen et al., 2009, Kopytova et al., 2008, Gandille et al., 2007, Comet et al., 2006, Kavi et al., 2006, Klymenko et al., 2006, Kopytova et al., 2006, Martinez et al., 2006, Chanas and Maschat, 2005, Kim et al., 2005, Lehmann, 2004, Narbonne et al., 2004, Narbonne et al., 2004, Bloyer et al., 2003, Boivin et al., 2003, Chanas et al., 2003, Faucheux et al., 2003, Perrin et al., 2003, Calgaro et al., 2002, Josse et al., 2002, Maurange and Paro, 2002, Moshkin et al., 2002, Bajusz et al., 2001, Bloyer et al., 2001, Brock and van Lohuizen, 2001, Faucheux et al., 2001, Fauvarque et al., 2001, Hodgson et al., 2001, Lopez et al., 2001, Maschat et al., 2001, Mollaaghababa et al., 2001, Netter et al., 2001, O'Connell et al., 2001, Roseman et al., 2001, Ruhf et al., 2001, Simonova et al., 2001, Berry and Gehring, 2000, Boivin et al., 2000, Netter and Theodore, 2000, Randsholt et al., 2000, Biryukova et al., 1999, Bloyer et al., 1999, Cavalli, 1999, Docquier et al., 1999, Levis and Preczewski, 1999, Soldatov et al., 1999, Taillebourg and Dura, 1999, Belenkaya et al., 1998, Belenkaya et al., 1998, Boivin and Dura, 1998, Bornemann et al., 1998, Buchenau et al., 1998, Fauvarque and Gehring, 1998, Georgiev et al., 1998, Jenuwein et al., 1998, Kodjabachian et al., 1998, Kyba and Brock, 1998, Maschat et al., 1998, Mihaly et al., 1998, Paro, 1998, Peterson et al., 1998, Santamaria, 1998, Serrano and Maschat, 1998, Stankunas et al., 1998, Theodore et al., 1998, van Lohuizen, 1998, Bornemann et al., 1997, Dura and Boivin, 1997, Gould, 1997, Peterson et al., 1997, Pirrotta, 1997, Schultz et al., 1997, Shaffer et al., 1997, Henikoff, 1996, Kingston et al., 1996, Maschat and Serrano, 1996, Ronsseray et al., 1996, Tripoulas et al., 1996, Campbell et al., 1995, Chang et al., 1995, Fauvarque et al., 1995, Franke et al., 1995, Orlando and Paro, 1995, Pirrotta, 1995, Ponting, 1995, Simmonds et al., 1995, Simon, 1995, Aguade and Langley, 1994, Andrew and Scott, 1994, de Camillis and Brock, 1994, Fauvarque and Dura, 1994, Landecker et al., 1994, Lonie et al., 1994, Moehrle and Paro, 1994, Paro, 1994, Pirrotta and Rastelli, 1994, Saget and Randsholt, 1994, Botas, 1993, Jimenez and Modolell, 1993, Morata, 1993, Paro, 1993, Rastelli et al., 1993, Wu, 1993, Bienz, 1992, Cheng and Brock, 1992, DeCamillis et al., 1992, Epstein, 1992, Franke et al., 1992, Henikoff, 1992, Deatrick et al., 1991, Dessain and McGinnis, 1991, Merriam et al., 1991, Paro, 1990, Dura et al., 1987)
    ph-proximal
    Name Synonyms
    POLYHOMEOTIC
    Polyhomeotic Proximal
    Polyhomeotic-proximal
    polyhomeotic proxima
    Secondary FlyBase IDs
    • FBgn0003077
    • FBgn0029600
    • FBgn0029601
    Datasets (0)
    Study focus (0)
    Experimental Role
    Project
    Project Type
    Title
    References (424)