Q9W4S7 · MYC_DROME
- ProteinMyc protein
- GeneMyc
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids717 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Participates in the regulation of gene transcription (PubMed:16087886, PubMed:24173801, PubMed:24615015, PubMed:25858587, PubMed:25999153, PubMed:8929412).
Binds DNA in a non-specific manner, yet also specifically recognizes the core sequence CAC[GA]TG (PubMed:8929412).
Seems to activate the transcription of growth-related genes; required for cellular proliferation and growth (PubMed:16087886, PubMed:25858587, PubMed:25999153).
Functions in the TORC2-mediated regulation of cell growth, acting downstream of the TORC2 complex (PubMed:25999153).
Inhibits the demethylase activity of Lid (PubMed:17311883).
Activates transcription of mbm (PubMed:24615015).
Has a role in ribosome biogenesis and endoreplication in fat body cells by activating the transcription of LTV1 (PubMed:25858587).
Able to induce the SCF E3 ubiquitin-protein ligase member archipelago (ago) which functions in its degradation (PubMed:15182669, PubMed:24173801).
It may therefore create a negative feedback loop with ago that is regulated by the ubiquitin hydrolase puf (PubMed:24173801).
In dopaminergic neurons, regulates dopamine levels by binding to the E-box (E1) of the dopamine decarboxylase Ddc promoter and thereby inhibiting its transcription (PubMed:35167135).
This regulation is required to suppress male-male courtship (PubMed:35167135).
Binds DNA in a non-specific manner, yet also specifically recognizes the core sequence CAC[GA]TG (PubMed:8929412).
Seems to activate the transcription of growth-related genes; required for cellular proliferation and growth (PubMed:16087886, PubMed:25858587, PubMed:25999153).
Functions in the TORC2-mediated regulation of cell growth, acting downstream of the TORC2 complex (PubMed:25999153).
Inhibits the demethylase activity of Lid (PubMed:17311883).
Activates transcription of mbm (PubMed:24615015).
Has a role in ribosome biogenesis and endoreplication in fat body cells by activating the transcription of LTV1 (PubMed:25858587).
Able to induce the SCF E3 ubiquitin-protein ligase member archipelago (ago) which functions in its degradation (PubMed:15182669, PubMed:24173801).
It may therefore create a negative feedback loop with ago that is regulated by the ubiquitin hydrolase puf (PubMed:24173801).
In dopaminergic neurons, regulates dopamine levels by binding to the E-box (E1) of the dopamine decarboxylase Ddc promoter and thereby inhibiting its transcription (PubMed:35167135).
This regulation is required to suppress male-male courtship (PubMed:35167135).
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMyc protein
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ9W4S7
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
RNAi-mediated knockdown in the neurons, only dopaminergic neurons or only adult neurons increases transcription of the dopamine decarboxylase Ddc and thereby dopamine concentration (PubMed:35167135).
In addition, induces male courtship propensity towards other males without altering male sexual preference towards females (PubMed:35167135).
RNAi-mediated knockdown in muscle or fat body does not elicit male-male courtship (PubMed:35167135).
Simultaneous knockdown of Ddc and myc restores increased dopamine levels and the induced male-male courtship observed in the single myc knockdown (PubMed:35167135).
Simultaneous knockdown of dopamine receptor Dop1R1 and myc restores the induced male-male courtship observed in the single myc knockdown (PubMed:35167135).
In addition, induces male courtship propensity towards other males without altering male sexual preference towards females (PubMed:35167135).
RNAi-mediated knockdown in muscle or fat body does not elicit male-male courtship (PubMed:35167135).
Simultaneous knockdown of Ddc and myc restores increased dopamine levels and the induced male-male courtship observed in the single myc knockdown (PubMed:35167135).
Simultaneous knockdown of dopamine receptor Dop1R1 and myc restores the induced male-male courtship observed in the single myc knockdown (PubMed:35167135).
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000127322 | 1-717 | Myc protein | |||
Sequence: MALYRSDPYSIMDDQLFSNISIFDMDNDLYDMDKLLSSSTIQSDLEKIEDMESVFQDYDLEEDMKPEIRNIDCMWPAMSSCLTSGNGNGIESGNSAASSYSETGAVSLAMVSGSTNLYSAYQRSQTTDNTQSNQQHVVNSAENMPVIIKKELADLDYTVCQKRLRLSGGDKKSQIQDEVHLIPPGGSLLRKRNNQDIIRKSGELSGSDSIKYQRPDTPHSLTDEVAASEFRHNVDLRACVMGSNNISLTGNDSDVNYIKQISRELQNTGKDPLPVRYIPPINDVLDVLNQHSNSTGGQQQLNQQQLDEQQQAIDIATGRNTVDSPPTTGSDSDSDDGEPLNFDLRHHRTSKSGSNASITTNNNNSNNKNNKLKNNSNGMLHMMHITDHSYTRCNDMVDDGPNLETPSDSDEEIDVVSYTDKKLPTNPSCHLMGALQFQMAHKISIDHMKQKPRYNNFNLPYTPASSSPVKSVANSRYPSPSSTPYQNCSSASPSYSPLSVDSSNVSSSSSSSSSQSSFTTSSSNKGRKRSSLKDPGLLISSSSVYLPGVNNKVTHSSMMSKKSRGKKVVGTSSGNTSPISSGQDVDAMDRNWQRRSGGIATSTSSNSSVHRKDFVLGFDEADTIEKRNQHNDMERQRRIGLKNLFEALKKQIPTIRDKERAPKVNILREAAKLCIQLTQEEKELSMQRQLLSLQLKQRQDTLASYQMELNESRSVSG | ||||||
Modified residue | 217 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 220 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Probably targeted for ubiquitination by the SFC ubiquitin ligase complex member ago, leading to its proteasomal degradation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Low levels detected throughout embryo before cellular blastoderm formation, particularly concentrated in pole plasm. Zygotic expression detected during cellular blastoderm stage in endodermal anlagen of anterior and posterior midgut at both poles. After gastrulation, expression detected in invaginating ventral furrow of mesoderm. Continued expression in anterior and posterior midgut and mesoderm during germband extension. During late germ-band retraction, expression remains detectable in fusing midgut and presumed developing somatic musculature.
Developmental stage
Expressed both maternally and zygotically in embryos.
Gene expression databases
Interaction
Subunit
Efficient DNA binding requires dimerization with another bHLH protein (PubMed:8929412).
Binds DNA as a heterodimer with Max (PubMed:8929412).
Interacts with ago (PubMed:15182669, PubMed:24173801).
Interacts with lid (PubMed:17311883).
Part of a complex containing lid, Myc and ash2 (PubMed:17311883).
Component of a complex with pont and rept (PubMed:16087886).
Interacts with puf (PubMed:24173801).
Binds DNA as a heterodimer with Max (PubMed:8929412).
Interacts with ago (PubMed:15182669, PubMed:24173801).
Interacts with lid (PubMed:17311883).
Part of a complex containing lid, Myc and ash2 (PubMed:17311883).
Component of a complex with pont and rept (PubMed:16087886).
Interacts with puf (PubMed:24173801).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9W4S7 | ago Q9VZF4 | 2 | EBI-120162, EBI-138334 | |
BINARY | Q9W4S7 | gro P16371 | 3 | EBI-120162, EBI-153866 | |
BINARY | Q9W4S7 | gro P16371-2 | 3 | EBI-120162, EBI-15661898 | |
BINARY | Q9W4S7 | Max P91664 | 3 | EBI-120162, EBI-193577 | |
BINARY | Q9W4S7 | pont Q9VH07 | 4 | EBI-120162, EBI-234957 | |
BINARY | Q9W4S7 | rept Q9V3K3 | 4 | EBI-120162, EBI-192924 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 288-335 | Polar residues | ||||
Sequence: LNQHSNSTGGQQQLNQQQLDEQQQAIDIATGRNTVDSPPTTGSDSDSD | ||||||
Region | 288-376 | Disordered | ||||
Sequence: LNQHSNSTGGQQQLNQQQLDEQQQAIDIATGRNTVDSPPTTGSDSDSDDGEPLNFDLRHHRTSKSGSNASITTNNNNSNNKNNKLKNNS | ||||||
Compositional bias | 351-376 | Polar residues | ||||
Sequence: KSGSNASITTNNNNSNNKNNKLKNNS | ||||||
Compositional bias | 462-526 | Polar residues | ||||
Sequence: TPASSSPVKSVANSRYPSPSSTPYQNCSSASPSYSPLSVDSSNVSSSSSSSSSQSSFTTSSSNKG | ||||||
Region | 462-535 | Disordered | ||||
Sequence: TPASSSPVKSVANSRYPSPSSTPYQNCSSASPSYSPLSVDSSNVSSSSSSSSSQSSFTTSSSNKGRKRSSLKDP | ||||||
Region | 555-584 | Disordered | ||||
Sequence: HSSMMSKKSRGKKVVGTSSGNTSPISSGQD | ||||||
Compositional bias | 566-584 | Polar residues | ||||
Sequence: KKVVGTSSGNTSPISSGQD | ||||||
Domain | 625-677 | bHLH | ||||
Sequence: EKRNQHNDMERQRRIGLKNLFEALKKQIPTIRDKERAPKVNILREAAKLCIQL | ||||||
Coiled coil | 679-711 | |||||
Sequence: QEEKELSMQRQLLSLQLKQRQDTLASYQMELNE |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length717
- Mass (Da)79,308
- Last updated2002-10-01 v2
- ChecksumD6A74CF5D4B80150
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
M9PGK0 | M9PGK0_DROME | Myc | 717 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 288-335 | Polar residues | ||||
Sequence: LNQHSNSTGGQQQLNQQQLDEQQQAIDIATGRNTVDSPPTTGSDSDSD | ||||||
Compositional bias | 351-376 | Polar residues | ||||
Sequence: KSGSNASITTNNNNSNNKNNKLKNNS | ||||||
Sequence conflict | 353 | in Ref. 3; AAD00517 | ||||
Sequence: G → D | ||||||
Sequence conflict | 362 | in Ref. 3; AAD00517 | ||||
Sequence: N → S | ||||||
Sequence conflict | 365 | in Ref. 3; AAD00517 | ||||
Sequence: S → K | ||||||
Sequence conflict | 369-373 | in Ref. 3; AAD00517 | ||||
Sequence: NNKLK → IKNNN | ||||||
Compositional bias | 462-526 | Polar residues | ||||
Sequence: TPASSSPVKSVANSRYPSPSSTPYQNCSSASPSYSPLSVDSSNVSSSSSSSSSQSSFTTSSSNKG | ||||||
Compositional bias | 566-584 | Polar residues | ||||
Sequence: KKVVGTSSGNTSPISSGQD |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U77370 EMBL· GenBank· DDBJ | AAB39842.2 EMBL· GenBank· DDBJ | mRNA | ||
U81384 EMBL· GenBank· DDBJ | AAD00517.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014298 EMBL· GenBank· DDBJ | AAF45866.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL121800 EMBL· GenBank· DDBJ | CAD24780.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY058627 EMBL· GenBank· DDBJ | AAL13856.1 EMBL· GenBank· DDBJ | mRNA |