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Protein

Myc protein

Gene

dm

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Participates in the regulation of gene transcription. Binds DNA in a non-specific manner, yet also specifically recognizes the core sequence CAC[GA]TG. Seems to activate the transcription of growth-related genes; required for cellular proliferation and growth. Inhibits the demethylase activity of Lid (PubMed:17311883). Activates transcription of mbm (PubMed:24615015).5 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • sequence-specific DNA binding Source: FlyBase
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  • cell competition in a multicellular organism Source: FlyBase
  • cell proliferation Source: UniProtKB
  • DNA endoreduplication Source: FlyBase
  • embryo development ending in birth or egg hatching Source: UniProtKB
  • embryonic pattern specification Source: FlyBase
  • lipid homeostasis Source: FlyBase
  • negative regulation of Notch signaling pathway Source: FlyBase
  • neurogenesis Source: FlyBase
  • oogenesis Source: FlyBase
  • positive regulation of cell growth Source: FlyBase
  • positive regulation of cell size Source: FlyBase
  • positive regulation of developmental growth Source: FlyBase
  • positive regulation of growth Source: FlyBase
  • positive regulation of imaginal disc growth Source: FlyBase
  • positive regulation of multicellular organism growth Source: FlyBase
  • positive regulation of neurogenesis Source: FlyBase
  • positive regulation of peptide hormone secretion Source: FlyBase
  • positive regulation of transcription, DNA-templated Source: FlyBase
  • regulation of apoptotic process Source: FlyBase
  • regulation of autophagy Source: FlyBase
  • regulation of cell cycle Source: FlyBase
  • regulation of cell growth Source: FlyBase
  • regulation of cell size Source: FlyBase
  • regulation of glucose metabolic process Source: FlyBase
  • regulation of imaginal disc-derived wing size Source: FlyBase
  • regulation of organ growth Source: FlyBase
  • regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of trehalose metabolic process Source: FlyBase
  • response to starvation Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-DME-69202. Cyclin E associated events during G1/S transition.
R-DME-69656. Cyclin A:Cdk2-associated events at S phase entry.
SignaLinkiQ9W4S7.

Names & Taxonomyi

Protein namesi
Recommended name:
Myc protein
Alternative name(s):
Diminutive protein
dMyc1
Short name:
dMyc
Gene namesi
Name:dm
ORF Names:CG10798
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0262656. dm.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB-SubCell
  • protein complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 717717Myc proteinPRO_0000127322Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei217 – 2171Phosphothreonine1 Publication
Modified residuei220 – 2201Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9W4S7.

PTM databases

iPTMnetiQ9W4S7.

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

Expressed both maternally and zygotically in embryos.2 Publications

Gene expression databases

BgeeiQ9W4S7.
ExpressionAtlasiQ9W4S7. differential.
GenevisibleiQ9W4S7. DM.

Interactioni

Subunit structurei

Heterodimer with another bHLH proteins. Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with Max. Interacts with lid. Part of a complex containing lid, dm and ash2. Component of a complex with pont and rept.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
agoQ9VZF42EBI-120162,EBI-138334
pontQ9VH074EBI-120162,EBI-234957
reptQ9V3K34EBI-120162,EBI-192924

Protein-protein interaction databases

BioGridi57835. 39 interactions.
DIPiDIP-18847N.
IntActiQ9W4S7. 15 interactions.
MINTiMINT-976875.
STRINGi7227.FBpp0303995.

Structurei

3D structure databases

ProteinModelPortaliQ9W4S7.
SMRiQ9W4S7. Positions 626-702.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini625 – 67753bHLHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili679 – 71133Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi361 – 37717Asn-richAdd
BLAST
Compositional biasi465 – 608144Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IPD1. Eukaryota.
ENOG410XXWA. LUCA.
GeneTreeiENSGT00510000046414.
InParanoidiQ9W4S7.
KOiK04377.
OMAiSYTRCNE.
OrthoDBiEOG7M0NSZ.
PhylomeDBiQ9W4S7.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9W4S7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALYRSDPYS IMDDQLFSNI SIFDMDNDLY DMDKLLSSST IQSDLEKIED
60 70 80 90 100
MESVFQDYDL EEDMKPEIRN IDCMWPAMSS CLTSGNGNGI ESGNSAASSY
110 120 130 140 150
SETGAVSLAM VSGSTNLYSA YQRSQTTDNT QSNQQHVVNS AENMPVIIKK
160 170 180 190 200
ELADLDYTVC QKRLRLSGGD KKSQIQDEVH LIPPGGSLLR KRNNQDIIRK
210 220 230 240 250
SGELSGSDSI KYQRPDTPHS LTDEVAASEF RHNVDLRACV MGSNNISLTG
260 270 280 290 300
NDSDVNYIKQ ISRELQNTGK DPLPVRYIPP INDVLDVLNQ HSNSTGGQQQ
310 320 330 340 350
LNQQQLDEQQ QAIDIATGRN TVDSPPTTGS DSDSDDGEPL NFDLRHHRTS
360 370 380 390 400
KSGSNASITT NNNNSNNKNN KLKNNSNGML HMMHITDHSY TRCNDMVDDG
410 420 430 440 450
PNLETPSDSD EEIDVVSYTD KKLPTNPSCH LMGALQFQMA HKISIDHMKQ
460 470 480 490 500
KPRYNNFNLP YTPASSSPVK SVANSRYPSP SSTPYQNCSS ASPSYSPLSV
510 520 530 540 550
DSSNVSSSSS SSSSQSSFTT SSSNKGRKRS SLKDPGLLIS SSSVYLPGVN
560 570 580 590 600
NKVTHSSMMS KKSRGKKVVG TSSGNTSPIS SGQDVDAMDR NWQRRSGGIA
610 620 630 640 650
TSTSSNSSVH RKDFVLGFDE ADTIEKRNQH NDMERQRRIG LKNLFEALKK
660 670 680 690 700
QIPTIRDKER APKVNILREA AKLCIQLTQE EKELSMQRQL LSLQLKQRQD
710
TLASYQMELN ESRSVSG
Length:717
Mass (Da):79,308
Last modified:October 1, 2002 - v2
Checksum:iD6A74CF5D4B80150
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti353 – 3531G → D in AAD00517 (PubMed:9037036).Curated
Sequence conflicti362 – 3621N → S in AAD00517 (PubMed:9037036).Curated
Sequence conflicti365 – 3651S → K in AAD00517 (PubMed:9037036).Curated
Sequence conflicti369 – 3735NNKLK → IKNNN in AAD00517 (PubMed:9037036).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U77370 mRNA. Translation: AAB39842.2.
U81384 mRNA. Translation: AAD00517.1.
AE014298 Genomic DNA. Translation: AAF45866.2.
AL121800 Genomic DNA. Translation: CAD24780.1.
AY058627 mRNA. Translation: AAL13856.1.
RefSeqiNP_001259204.1. NM_001272275.1.
NP_525062.2. NM_080323.4.
UniGeneiDm.4239.

Genome annotation databases

EnsemblMetazoaiFBtr0070525; FBpp0070501; FBgn0262656.
FBtr0331605; FBpp0303995; FBgn0262656.
GeneIDi31310.
KEGGidme:Dmel_CG10798.
UCSCiCG10798-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U77370 mRNA. Translation: AAB39842.2.
U81384 mRNA. Translation: AAD00517.1.
AE014298 Genomic DNA. Translation: AAF45866.2.
AL121800 Genomic DNA. Translation: CAD24780.1.
AY058627 mRNA. Translation: AAL13856.1.
RefSeqiNP_001259204.1. NM_001272275.1.
NP_525062.2. NM_080323.4.
UniGeneiDm.4239.

3D structure databases

ProteinModelPortaliQ9W4S7.
SMRiQ9W4S7. Positions 626-702.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi57835. 39 interactions.
DIPiDIP-18847N.
IntActiQ9W4S7. 15 interactions.
MINTiMINT-976875.
STRINGi7227.FBpp0303995.

PTM databases

iPTMnetiQ9W4S7.

Proteomic databases

PaxDbiQ9W4S7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070525; FBpp0070501; FBgn0262656.
FBtr0331605; FBpp0303995; FBgn0262656.
GeneIDi31310.
KEGGidme:Dmel_CG10798.
UCSCiCG10798-RA. d. melanogaster.

Organism-specific databases

CTDi4609.
FlyBaseiFBgn0262656. dm.

Phylogenomic databases

eggNOGiENOG410IPD1. Eukaryota.
ENOG410XXWA. LUCA.
GeneTreeiENSGT00510000046414.
InParanoidiQ9W4S7.
KOiK04377.
OMAiSYTRCNE.
OrthoDBiEOG7M0NSZ.
PhylomeDBiQ9W4S7.

Enzyme and pathway databases

ReactomeiR-DME-69202. Cyclin E associated events during G1/S transition.
R-DME-69656. Cyclin A:Cdk2-associated events at S phase entry.
SignaLinkiQ9W4S7.

Miscellaneous databases

ChiTaRSidm. fly.
GenomeRNAii31310.
PROiQ9W4S7.

Gene expression databases

BgeeiQ9W4S7.
ExpressionAtlasiQ9W4S7. differential.
GenevisibleiQ9W4S7. DM.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Oregon-R1 Publication.
  2. Gallant P., Shiio Y., Cheng P.F., Parkhurst S.M., Eisenman R.N.
    Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 274.
  3. "Drosophila Myc is oncogenic in mammalian cells and plays a role in the diminutive phenotype."
    Schreiber-Agus N., Stein D., Chen K., Goltz J.S., Stevens L., DePinho R.A.
    Proc. Natl. Acad. Sci. U.S.A. 94:1235-1240(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  4. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Oregon-R1 Publication.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication.
  8. "The Drosophila F box protein archipelago regulates dMyc protein levels in vivo."
    Moberg K.H., Mukherjee A., Veraksa A., Artavanis-Tsakonas S., Hariharan I.K.
    Curr. Biol. 14:965-974(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AGO.
  9. "Myc interacts genetically with Tip48/Reptin and Tip49/Pontin to control growth and proliferation during Drosophila development."
    Bellosta P., Hulf T., Balla Diop S., Usseglio F., Pradel J., Aragnol D., Gallant P.
    Proc. Natl. Acad. Sci. U.S.A. 102:11799-11804(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PONT AND REPT.
  10. "The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase required for dMyc-induced cell growth."
    Secombe J., Li L., Carlos L., Eisenman R.N.
    Genes Dev. 21:537-551(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LID, IDENTIFICATION IN COMPLEX WITH LID AND ASH2.
  11. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217 AND SER-220, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  12. "Drosophila mbm is a nucleolar myc and casein kinase 2 target required for ribosome biogenesis and cell growth of central brain neuroblasts."
    Hovhanyan A., Herter E.K., Pfannstiel J., Gallant P., Raabe T.
    Mol. Cell. Biol. 34:1878-1891(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiMYC_DROME
AccessioniPrimary (citable) accession number: Q9W4S7
Secondary accession number(s): O96903, P91665
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: October 1, 2002
Last modified: July 6, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

Targeted by archipelago for degradation by the SFC ubiquitin ligase complex.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.