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Protein

Myb protein

Gene

Myb

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

Functioni

DNA-binding protein that specifically recognizes the sequence 5'-YAAC[GT]G-3'. Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. In follicle cells, the complex plays a central role in the site-specific DNA replication at the chorion loci. During development, the complex represses transcription of developmentally controlled E2F target genes.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi159 – 18224H-T-H motifPROSITE-ProRule annotationAdd
BLAST
DNA bindingi210 – 23324H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: FlyBase
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: FlyBase
  • transcription factor activity, sequence-specific DNA binding Source: FlyBase

GO - Biological processi

  • cell proliferation Source: FlyBase
  • centriole replication Source: FlyBase
  • centrosome cycle Source: FlyBase
  • centrosome organization Source: FlyBase
  • chromosome condensation Source: FlyBase
  • eggshell chorion gene amplification Source: FlyBase
  • Golgi organization Source: FlyBase
  • mitotic cell cycle Source: FlyBase
  • mitotic cytokinesis Source: FlyBase
  • mitotic nuclear division Source: FlyBase
  • mitotic spindle assembly Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • negative regulation of cell size Source: FlyBase
  • positive regulation of cell proliferation Source: FlyBase
  • positive regulation of G2/M transition of mitotic cell cycle Source: FlyBase
  • positive regulation of mitotic cell cycle Source: FlyBase
  • positive regulation of transcription involved in G2/M transition of mitotic cell cycle Source: FlyBase
  • regulation of glucose metabolic process Source: FlyBase
  • regulation of mitotic nuclear division Source: FlyBase
  • spindle organization Source: FlyBase
  • transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

SignaLinkiP04197.

Names & Taxonomyi

Protein namesi
Recommended name:
Myb protein
Gene namesi
Name:Myb
ORF Names:CG9045
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0002914. Myb.

Subcellular locationi

GO - Cellular componenti

  • Myb complex Source: FlyBase
  • nuclear euchromatin Source: FlyBase
  • nucleus Source: FlyBase
  • polytene chromosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 657657Myb proteinPRO_0000197052Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei381 – 3811Phosphoserine1 Publication
Modified residuei389 – 3891Phosphoserine1 Publication
Modified residuei396 – 3961Phosphoserine1 Publication
Modified residuei445 – 4451Phosphothreonine1 Publication
Modified residuei447 – 4471Phosphothreonine1 Publication
Modified residuei557 – 5571Phosphothreonine1 Publication
Modified residuei558 – 5581Phosphoserine1 Publication
Modified residuei566 – 5661Phosphothreonine1 Publication
Modified residuei569 – 5691Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP04197.
PRIDEiP04197.

PTM databases

iPTMnetiP04197.

Expressioni

Gene expression databases

BgeeiP04197.
ExpressionAtlasiP04197. differential.
GenevisibleiP04197. DM.

Interactioni

Subunit structurei

Component of the DREAM complex at least composed of Myb, Caf1, mip40, mip120, mip130, E2f2, Dp, Rbf, Rbf2, lin-52, Rpd3 and l3mbt.3 Publications

Protein-protein interaction databases

BioGridi58891. 13 interactions.
DIPiDIP-22816N.
IntActiP04197. 11 interactions.
MINTiMINT-282433.
STRINGi7227.FBpp0089402.

Structurei

3D structure databases

ProteinModelPortaliP04197.
SMRiP04197. Positions 87-236.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini87 – 13044HTH myb-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini131 – 18656HTH myb-type 2PROSITE-ProRule annotationAdd
BLAST
Domaini187 – 23751HTH myb-type 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 3 HTH myb-type DNA-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0048. Eukaryota.
COG5147. LUCA.
InParanoidiP04197.
KOiK09420.
OMAiSSIETPH.
OrthoDBiEOG7M98G6.
PhylomeDBiP04197.

Family and domain databases

Gene3Di1.10.10.60. 3 hits.
InterProiIPR015395. C-myb_C.
IPR009057. Homeodomain-like.
IPR017877. Myb-like_dom.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
[Graphical view]
PfamiPF09316. Cmyb_C. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]
SMARTiSM00717. SANT. 3 hits.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
PROSITEiPS51294. HTH_MYB. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04197-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASASTENGE ELMNYGSNSD SEESEYSENE DTQVCDKDSQ QNSNADSGYP
60 70 80 90 100
LDSPELQDSK TTGQKGQNKS GKTSIGAVHP NYGFGKRWSK SEDVLLKQLV
110 120 130 140 150
ETHGENWEII GPHFKDRLEQ QVQQRWAKVL NPELIKGPWT RDEDDMVIKL
160 170 180 190 200
VRNFGPKKWT LIARYLNGRI GKQCRERWHN HLNPNIKKTA WTEKEDEIIY
210 220 230 240 250
QAHLELGNQW AKIAKRLPGR TDNAIKNHWN STMRRKYDVE RRSVNASGSD
260 270 280 290 300
LKSSRTHLIT LIKSGGISKC MNNMQHNKES GGEAVNKSEN ADGASVTAVK
310 320 330 340 350
GGDLAQESQD DHQKGSNLAH LSMQHLIKLT MPRQTPIILK RTRKHIPETH
360 370 380 390 400
HQAGCSSSET FNQEEAAGNA RSRPPSSPVI SPIKSLPFSP SHFLKSPCLT
410 420 430 440 450
TFEDMDLRAS TPVTKVYNRV GMEIKKEMET SSIETPHKSQ LGPRTPTPFK
460 470 480 490 500
KALAAIGKKR DGRRYEPSSP SSLVEDLAEI IHEEHLSNSL TANNSKMMGA
510 520 530 540 550
ADQNSTLSTE YNAQSPPHMK RARKSLLSTW SSNHPYNAGS AKRIQPFETE
560 570 580 590 600
TPSKFLTSPG DILKDTLCSE QDLPFDEGRK ENRPFHNRRI NKYRGGLTYD
610 620 630 640 650
HVIDPKWARV ACGKSRDQMF MEEQAYACLK NLSCISRSLN FEKQKCLVNS

FDRFGSL
Length:657
Mass (Da):74,045
Last modified:June 1, 2001 - v2
Checksum:i8265B37ABB250AE4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti370 – 3701A → V in CAA29373 (PubMed:3121304).Curated
Sequence conflicti440 – 4412QL → KY in AAA70367 (PubMed:3921261).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05939 mRNA. Translation: CAA29373.1.
AE014298 Genomic DNA. Translation: AAF48529.1.
M11281 Genomic DNA. Translation: AAA70367.1.
PIRiS00578. TVFFMA.
RefSeqiNP_511170.1. NM_078615.4.
NP_996454.1. NM_206731.2.
NP_996456.1. NM_206733.2.
NP_996457.1. NM_206734.2.
UniGeneiDm.2907.

Genome annotation databases

EnsemblMetazoaiFBtr0074169; FBpp0073961; FBgn0002914.
FBtr0074170; FBpp0089402; FBgn0002914.
FBtr0074171; FBpp0089403; FBgn0002914.
FBtr0074173; FBpp0089405; FBgn0002914.
GeneIDi32543.
KEGGidme:Dmel_CG9045.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05939 mRNA. Translation: CAA29373.1.
AE014298 Genomic DNA. Translation: AAF48529.1.
M11281 Genomic DNA. Translation: AAA70367.1.
PIRiS00578. TVFFMA.
RefSeqiNP_511170.1. NM_078615.4.
NP_996454.1. NM_206731.2.
NP_996456.1. NM_206733.2.
NP_996457.1. NM_206734.2.
UniGeneiDm.2907.

3D structure databases

ProteinModelPortaliP04197.
SMRiP04197. Positions 87-236.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58891. 13 interactions.
DIPiDIP-22816N.
IntActiP04197. 11 interactions.
MINTiMINT-282433.
STRINGi7227.FBpp0089402.

PTM databases

iPTMnetiP04197.

Proteomic databases

PaxDbiP04197.
PRIDEiP04197.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0074169; FBpp0073961; FBgn0002914.
FBtr0074170; FBpp0089402; FBgn0002914.
FBtr0074171; FBpp0089403; FBgn0002914.
FBtr0074173; FBpp0089405; FBgn0002914.
GeneIDi32543.
KEGGidme:Dmel_CG9045.

Organism-specific databases

CTDi4602.
FlyBaseiFBgn0002914. Myb.

Phylogenomic databases

eggNOGiKOG0048. Eukaryota.
COG5147. LUCA.
InParanoidiP04197.
KOiK09420.
OMAiSSIETPH.
OrthoDBiEOG7M98G6.
PhylomeDBiP04197.

Enzyme and pathway databases

SignaLinkiP04197.

Miscellaneous databases

GenomeRNAii32543.
PROiP04197.

Gene expression databases

BgeeiP04197.
ExpressionAtlasiP04197. differential.
GenevisibleiP04197. DM.

Family and domain databases

Gene3Di1.10.10.60. 3 hits.
InterProiIPR015395. C-myb_C.
IPR009057. Homeodomain-like.
IPR017877. Myb-like_dom.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
[Graphical view]
PfamiPF09316. Cmyb_C. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]
SMARTiSM00717. SANT. 3 hits.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
PROSITEiPS51294. HTH_MYB. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Drosophila and vertebrate myb proteins share two conserved regions, one of which functions as a DNA-binding domain."
    Peters C.W.B., Sippel A.E., Vingron M., Klempnauer K.-H.
    EMBO J. 6:3085-3090(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Oregon-R.
  2. "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: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "Isolation of the proto-oncogene c-myb from D. melanogaster."
    Katzen A.L., Kornberg T.B., Bishop J.M.
    Cell 41:449-456(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-441.
  5. "Role for a Drosophila Myb-containing protein complex in site-specific DNA replication."
    Beall E.L., Manak J.R., Zhou S., Bell M., Lipsick J.S., Botchan M.R.
    Nature 420:833-837(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE DREAM COMPLEX.
  6. "Native E2F/RBF complexes contain Myb-interacting proteins and repress transcription of developmentally controlled E2F target genes."
    Korenjak M., Taylor-Harding B., Binne U.K., Satterlee J.S., Stevaux O., Aasland R., White-Cooper H., Dyson N., Brehm A.
    Cell 119:181-193(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE DREAM COMPLEX.
  7. "Identification of a Drosophila Myb-E2F2/RBF transcriptional repressor complex."
    Lewis P.W., Beall E.L., Fleischer T.C., Georlette D., Link A.J., Botchan M.R.
    Genes Dev. 18:2929-2940(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
  8. "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 SER-381; SER-389; SER-396; THR-445; THR-447; THR-557; SER-558; THR-566 AND SER-569, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiMYB_DROME
AccessioniPrimary (citable) accession number: P04197
Secondary accession number(s): Q9VXM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

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.