N
Gene Ontology Biological Process
- I-kappaB phosphorylation [IMP]
- Malpighian tubule tip cell differentiation [IMP]
- Notch signaling pathway [NAS]
- R1/R6 cell differentiation [IMP]
- R3/R4 cell fate commitment [NAS]
- R7 cell differentiation [IMP, TAS]
- R8 cell development [TAS]
- R8 cell differentiation [NAS]
- R8 cell fate commitment [TAS]
- actin filament organization [IMP]
- anesthesia-resistant memory [IMP]
- anterior/posterior pattern specification [TAS]
- asymmetric cell division [TAS]
- axon guidance [IMP]
- border follicle cell migration [IMP]
- cell adhesion [TAS]
- cell fate commitment [NAS]
- cell fate specification [NAS, TAS]
- chaeta development [IMP]
- chaeta morphogenesis [IMP]
- compound eye cone cell fate commitment [TAS]
- compound eye development [IMP, NAS, TAS]
- compound eye morphogenesis [IMP]
- compound eye retinal cell programmed cell death [TAS]
- crystal cell differentiation [IMP]
- determination of adult lifespan [IMP]
- dorsal appendage formation [IMP]
- dorsal closure [TAS]
- dorsal/ventral lineage restriction, imaginal disc [TAS]
- dorsal/ventral pattern formation, imaginal disc [TAS]
- ectoderm development [TAS]
- embryonic crystal cell differentiation [TAS]
- embryonic hemopoiesis [IMP]
- epithelial cell proliferation involved in Malpighian tubule morphogenesis [IMP]
- epithelial cell type specification, open tracheal system [IMP]
- epithelium development [IMP]
- establishment of imaginal disc-derived wing hair orientation [NAS]
- establishment of ommatidial planar polarity [NAS, TAS]
- eye-antennal disc development [IMP]
- foregut morphogenesis [IMP]
- formation of a compartment boundary [IMP]
- germ-line stem cell maintenance [IMP]
- germarium-derived egg chamber formation [IMP, TAS]
- germarium-derived female germ-line cyst encapsulation [TAS]
- germarium-derived female germ-line cyst formation [IMP]
- glial cell differentiation [IMP]
- glial cell fate determination [IMP]
- glial cell migration [IMP]
- hemocyte proliferation [IMP]
- heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [IDA, IMP]
- imaginal disc growth [TAS]
- imaginal disc pattern formation [TAS]
- imaginal disc-derived leg joint morphogenesis [IMP]
- imaginal disc-derived leg segmentation [IMP]
- imaginal disc-derived male genitalia morphogenesis [IMP]
- imaginal disc-derived wing margin morphogenesis [IMP]
- imaginal disc-derived wing morphogenesis [IMP, NAS]
- imaginal disc-derived wing vein specification [IMP]
- intestinal stem cell homeostasis [IMP]
- lamellocyte differentiation [IMP]
- larval lymph gland hemopoiesis [IMP]
- lateral inhibition [IMP, NAS, TAS]
- leg disc morphogenesis [TAS]
- long-term memory [IGI, IMP]
- lymph gland crystal cell differentiation [TAS]
- lymph gland development [IMP]
- mesoderm development [IMP]
- morphogenesis of follicular epithelium [NAS]
- motor neuron axon guidance [IMP]
- muscle cell fate determination [IMP]
- negative regulation of JNK cascade [NAS]
- negative regulation of compound eye photoreceptor development [IMP]
- negative regulation of fusion cell fate specification [TAS]
- negative regulation of gene expression [IMP]
- negative regulation of neurogenesis [IMP]
- negative regulation of terminal cell fate specification, open tracheal system [TAS]
- negative regulation of transcription from RNA polymerase II promoter [TAS]
- neuroblast fate determination [IDA]
- neurological system process [IMP]
- neuron development [IMP]
- oocyte anterior/posterior axis specification [TAS]
- oocyte localization involved in germarium-derived egg chamber formation [IMP]
- oogenesis [IMP]
- open tracheal system development [TAS]
- ovarian follicle cell development [IMP, TAS]
- ovarian follicle cell migration [IMP]
- ovarian follicle cell stalk formation [IMP, TAS]
- peripheral nervous system development [IMP, TAS]
- positive regulation of G1/S transition of mitotic cell cycle [IMP]
- positive regulation of Notch signaling pathway [IMP]
- positive regulation of cell proliferation [IMP]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- regulation of R8 cell spacing in compound eye [NAS]
- regulation of cardioblast cell fate specification [IMP]
- regulation of cell differentiation [IMP]
- regulation of crystal cell differentiation [TAS]
- regulation of filopodium assembly [IMP]
- regulation of growth [IGI, IMP]
- regulation of mitotic cell cycle [TAS]
- regulation of neurogenesis [IMP]
- response to symbiont [IMP]
- retinal cell programmed cell death [TAS]
- second mitotic wave involved in compound eye morphogenesis [IMP, NAS]
- sensory organ development [IMP]
- sensory organ precursor cell fate determination [IMP]
- skeletal muscle tissue development [IMP]
- stem cell differentiation [IMP]
- ventral cord development [NAS]
- wing disc dorsal/ventral pattern formation [IMP]
- wing disc pattern formation [IMP]
- wing disc proximal/distal pattern formation [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- adherens junction [IDA]
- cell surface [IDA]
- cytoplasm [IDA]
- cytoplasmic vesicle [IDA]
- endocytic vesicle [IDA]
- endosome [IDA]
- integral component of membrane [TAS]
- integral component of plasma membrane [NAS]
- intracellular [IDA, NAS]
- late endosome [IDA]
- lysosome [IDA]
- nucleus [IDA, NAS, TAS]
- plasma membrane [IDA]
- protein complex [IPI]
- subapical complex [IDA]
SU(H)
Gene Ontology Biological Process
- I-kappaB phosphorylation [IMP]
- Notch signaling pathway [IGI, IMP, NAS, TAS]
- asymmetric cell division [TAS]
- cell fate determination [TAS]
- crystal cell differentiation [IMP]
- dorsal/ventral lineage restriction, imaginal disc [NAS]
- hemopoiesis [TAS]
- imaginal disc-derived wing vein morphogenesis [IMP]
- lateral inhibition [TAS]
- long-term memory [IMP]
- negative regulation of compound eye cone cell fate specification [TAS]
- negative regulation of transcription from RNA polymerase II promoter [IGI]
- negative regulation of transcription, DNA-templated [TAS]
- positive regulation of G1/S transition of mitotic cell cycle [IMP]
- positive regulation of transcription from RNA polymerase II promoter [TAS]
- positive regulation of transcription, DNA-templated [TAS]
- sensory organ precursor cell fate determination [IMP]
- wing disc dorsal/ventral pattern formation [IGI]
Gene Ontology Molecular Function- DNA binding [IDA, NAS, TAS]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [IGI]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IDA, IMP]
- RNA polymerase II distal enhancer sequence-specific DNA binding [IDA]
- protein binding [IPI]
- sequence-specific DNA binding [IDA]
- DNA binding [IDA, NAS, TAS]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [IGI]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IDA, IMP]
- RNA polymerase II distal enhancer sequence-specific DNA binding [IDA]
- protein binding [IPI]
- sequence-specific DNA binding [IDA]
Gene Ontology Cellular Component
Two-hybrid
Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.
Publication
The Drosophila importin-α3 is required for nuclear import of notch in vivo and it displays synergistic effects with notch receptor on cell proliferation.
The Notch signaling pathway controls diverse cell-fate specification events throughout development. The versatility of this pathway to influence different aspects of development comes from its multiple levels of regulation. Upon ligand-induced Notch activation, the Notch intracellular domain (Notch-ICD) is released from the membrane and translocates to the nucleus, where it transduces Notch signals by regulating the transcription of downstream target ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| N SU(H) | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | High | - | FlyBase | - | |
| SU(H) N | Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | FlyBase | - | |
| SU(H) N | Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | FlyBase | - | |
| SU(H) N | Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | FlyBase | - | |
| SU(H) N | Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | FlyBase | - | |
| SU(H) N | Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | FlyBase | - | |
| N SU(H) | Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | FlyBase | - | |
| SU(H) N | Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | FlyBase | - | |
| N SU(H) | Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex. | Low | - | FlyBase | - | |
| N SU(H) | Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex. | Low | - | FlyBase | - | |
| N SU(H) | Phenotypic Enhancement Phenotypic Enhancement A genetic interaction is inferred when mutation or overexpression of one gene results in enhancement of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene. | Low | - | FlyBase | - | |
| SU(H) N | Phenotypic Enhancement Phenotypic Enhancement A genetic interaction is inferred when mutation or overexpression of one gene results in enhancement of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene. | Low | - | FlyBase | - | |
| N SU(H) | Phenotypic Enhancement Phenotypic Enhancement A genetic interaction is inferred when mutation or overexpression of one gene results in enhancement of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene. | Low | - | FlyBase | - | |
| N SU(H) | Phenotypic Enhancement Phenotypic Enhancement A genetic interaction is inferred when mutation or overexpression of one gene results in enhancement of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene. | Low | - | FlyBase | - | |
| N SU(H) | Phenotypic Enhancement Phenotypic Enhancement A genetic interaction is inferred when mutation or overexpression of one gene results in enhancement of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene. | Low | - | FlyBase | - | |
| N SU(H) | Phenotypic Enhancement Phenotypic Enhancement A genetic interaction is inferred when mutation or overexpression of one gene results in enhancement of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene. | Low | - | FlyBase | - | |
| N SU(H) | Phenotypic Enhancement Phenotypic Enhancement A genetic interaction is inferred when mutation or overexpression of one gene results in enhancement of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene. | Low | - | FlyBase | - | |
| N SU(H) | Phenotypic Suppression Phenotypic Suppression A genetic interaction is inferred when mutation or over expression of one gene results in suppression of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene. | Low | - | FlyBase | - | |
| N SU(H) | Phenotypic Suppression Phenotypic Suppression A genetic interaction is inferred when mutation or over expression of one gene results in suppression of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene. | Low | - | FlyBase | - | |
| N SU(H) | Phenotypic Suppression Phenotypic Suppression A genetic interaction is inferred when mutation or over expression of one gene results in suppression of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene. | Low | - | FlyBase | - | |
| N SU(H) | Phenotypic Suppression Phenotypic Suppression A genetic interaction is inferred when mutation or over expression of one gene results in suppression of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene. | Low | - | FlyBase | - | |
| N SU(H) | Phenotypic Suppression Phenotypic Suppression A genetic interaction is inferred when mutation or over expression of one gene results in suppression of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene. | Low | - | FlyBase | - | |
| N SU(H) | Phenotypic Suppression Phenotypic Suppression A genetic interaction is inferred when mutation or over expression of one gene results in suppression of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene. | Low | - | FlyBase | - | |
| N SU(H) | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | FlyBase | - | |
| N SU(H) | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | FlyBase | - | |
| N SU(H) | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | FlyBase | - | |
| N SU(H) | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | FlyBase | - | |
| N SU(H) | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | FlyBase | - | |
| SU(H) N | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | FlyBase | - | |
| N SU(H) | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | FlyBase | - | |
| N SU(H) | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | High | - | BioGRID | 443547 | |
| N SU(H) | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | FlyBase | - | |
| N SU(H) | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | FlyBase | - | |
| N SU(H) | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | FlyBase | - | |
| N SU(H) | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | FlyBase | - | |
| N SU(H) | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | FlyBase | - | |
| N SU(H) | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | FlyBase | - | |
| N SU(H) | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | FlyBase | - | |
| SU(H) N | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | FlyBase | - | |
| N SU(H) | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | FlyBase | - |