Q9W4S7 (MYC_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myc protein

Alternative name(s):
Diminutive protein
dMyc1
Short name=dMyc

Gene names

Name:	dm
ORF Names:	CG10798

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	717 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.8 Ref.9 Ref.10
Subunit structure	Heterodimer with another bHLH proteins. Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as an heterodimer with Max. Interacts with lid. Part of a complex containing lid, dm and ash2. Component of a complex with pont and rept. Ref.1 Ref.8 Ref.9 Ref.10
Subcellular location	Nucleus.
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. Ref.1 Ref.3
Developmental stage	Expressed both maternally and zygotically in embryos. Ref.1 Ref.3
Miscellaneous	Targeted by archipelago for degradation by the SFC ubiquitin ligase complex.
Sequence similarities	Contains 1 basic helix-loop-helix (bHLH) domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Coiled coil
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell proliferation Inferred from expression pattern Ref.3. Source: UniProtKB embryo development ending in birth or egg hatching Inferred from expression pattern Ref.3. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from direct assay Ref.1. Source: UniProtKB protein binding Inferred from physical interaction Ref.9Ref.10. Source: UniProtKB sequence-specific DNA binding transcription factor activity Inferred from direct assay Ref.3. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ago	Q9VZF4	2	EBI-120162,EBI-138334
pont	Q9VH07	4	EBI-120162,EBI-234957
rept	Q9V3K3	4	EBI-120162,EBI-192924

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 717	717	Myc protein		PRO_0000127322
Regions
	Domain	639 – 678	40	Helix-loop-helix motif
	DNA binding	626 – 638	13	Basic motif
	Coiled coil	679 – 711	33	Potential
	Compositional bias	361 – 377	17	Asn-rich
	Compositional bias	465 – 608	144	Ser-rich
Amino acid modifications
	Modified residue	217	1	Phosphothreonine Ref.11
	Modified residue	220	1	Phosphoserine Ref.11
Experimental info
	Sequence conflict	353	1	G → D in AAD00517. Ref.3
	Sequence conflict	362	1	N → S in AAD00517. Ref.3
	Sequence conflict	365	1	S → K in AAD00517. Ref.3
	Sequence conflict	369 – 373	5	NNKLK → IKNNN in AAD00517. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9W4S7 [UniParc]. Last modified October 1, 2002. Version 2. Checksum: D6A74CF5D4B80150	FASTA	717	79,308
	10 20 30 40 50 60 MALYRSDPYS IMDDQLFSNI SIFDMDNDLY DMDKLLSSST IQSDLEKIED MESVFQDYDL 70 80 90 100 110 120 EEDMKPEIRN IDCMWPAMSS CLTSGNGNGI ESGNSAASSY SETGAVSLAM VSGSTNLYSA 130 140 150 160 170 180 YQRSQTTDNT QSNQQHVVNS AENMPVIIKK ELADLDYTVC QKRLRLSGGD KKSQIQDEVH 190 200 210 220 230 240 LIPPGGSLLR KRNNQDIIRK SGELSGSDSI KYQRPDTPHS LTDEVAASEF RHNVDLRACV 250 260 270 280 290 300 MGSNNISLTG NDSDVNYIKQ ISRELQNTGK DPLPVRYIPP INDVLDVLNQ HSNSTGGQQQ 310 320 330 340 350 360 LNQQQLDEQQ QAIDIATGRN TVDSPPTTGS DSDSDDGEPL NFDLRHHRTS KSGSNASITT 370 380 390 400 410 420 NNNNSNNKNN KLKNNSNGML HMMHITDHSY TRCNDMVDDG PNLETPSDSD EEIDVVSYTD 430 440 450 460 470 480 KKLPTNPSCH LMGALQFQMA HKISIDHMKQ KPRYNNFNLP YTPASSSPVK SVANSRYPSP 490 500 510 520 530 540 SSTPYQNCSS ASPSYSPLSV DSSNVSSSSS SSSSQSSFTT SSSNKGRKRS SLKDPGLLIS 550 560 570 580 590 600 SSSVYLPGVN NKVTHSSMMS KKSRGKKVVG TSSGNTSPIS SGQDVDAMDR NWQRRSGGIA 610 620 630 640 650 660 TSTSSNSSVH RKDFVLGFDE ADTIEKRNQH NDMERQRRIG LKNLFEALKK QIPTIRDKER 670 680 690 700 710 APKVNILREA AKLCIQLTQE EKELSMQRQL LSLQLKQRQD TLASYQMELN ESRSVSG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Myc and Max homologs in Drosophila." Gallant P., Shiio Y., Cheng P.F., Parkhurst S.M., Eisenman R.N. Science 274:1523-1527(1996) [PubMed: 8929412] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: Oregon-R.
[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: 9037036] [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: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[5]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[6]	"From sequence to chromosome: the tip of the X chromosome of D. melanogaster." Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., Minana B. , Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., Glover D.M. Science 287:2220-2222(2000) [PubMed: 10731137] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Oregon-R.
[7]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[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: 15182669] [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: 16087886] [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: 17311883] [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: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217 AND SER-220, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
RefSeq	NP_525062.2. NM_080323.2.
UniGene	Dm.4239.
3D structure databases
ProteinModelPortal	Q9W4S7.
SMR	Q9W4S7. Positions 625-706.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-18847N.
IntAct	Q9W4S7. 13 interactions.
MINT	MINT-976875.
STRING	Q9W4S7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0070525; FBpp0070501; FBgn0262656.
GeneID	31310.
KEGG	dme:Dmel_CG10798.
NMPDR	fig|7227.3.peg.16361.
UCSC	CG10798-RA. d. melanogaster.
Organism-specific databases
CTD	13399.
FlyBase	FBgn0262656. dm.
Phylogenomic databases
eggNOG	meNOG14068.
GeneTree	EMGT00050000002066.
InParanoid	Q9W4S7.
OMA	DHSYTRC.
OrthoDB	EOG48SF8B.
PhylomeDB	Q9W4S7.
Gene expression databases
ArrayExpress	Q9W4S7.
Bgee	Q9W4S7.
GermOnline	CG10798. Drosophila melanogaster.
Family and domain databases
InterPro	IPR011598. HLH_DNA-bd. [Graphical view]
Gene3D	G3DSA:4.10.280.10. HLH_DNA_bd. 1 hit.
Pfam	PF00010. HLH. 1 hit. [Graphical view]
SMART	SM00353. HLH. 1 hit. [Graphical view]
SUPFAM	SSF47459. HLH_basic. 1 hit.
PROSITE	PS50888. HLH. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	772984.

Entry information

Entry name

MYC_DROME

Accession

Primary (citable) accession number: Q9W4S7
Secondary accession number(s): O96903, P91665

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project