MYB_DROME
ID MYB_DROME Reviewed; 657 AA.
AC P04197; Q9VXM9;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Myb protein;
GN Name=Myb; ORFNames=CG9045;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Oregon-R;
RX PubMed=3121304; DOI=10.1002/j.1460-2075.1987.tb02616.x;
RA Peters C.W.B., Sippel A.E., Vingron M., Klempnauer K.-H.;
RT "Drosophila and vertebrate myb proteins share two conserved regions, one of
RT which functions as a DNA-binding domain.";
RL EMBO J. 6:3085-3090(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-441.
RX PubMed=3921261; DOI=10.1016/s0092-8674(85)80018-0;
RA Katzen A.L., Kornberg T.B., Bishop J.M.;
RT "Isolation of the proto-oncogene c-myb from D. melanogaster.";
RL Cell 41:449-456(1985).
RN [5]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP DREAM COMPLEX.
RX PubMed=12490953; DOI=10.1038/nature01228;
RA Beall E.L., Manak J.R., Zhou S., Bell M., Lipsick J.S., Botchan M.R.;
RT "Role for a Drosophila Myb-containing protein complex in site-specific DNA
RT replication.";
RL Nature 420:833-837(2002).
RN [6]
RP FUNCTION, AND IDENTIFICATION IN THE DREAM COMPLEX.
RX PubMed=15479636; DOI=10.1016/j.cell.2004.09.034;
RA Korenjak M., Taylor-Harding B., Binne U.K., Satterlee J.S., Stevaux O.,
RA Aasland R., White-Cooper H., Dyson N., Brehm A.;
RT "Native E2F/RBF complexes contain Myb-interacting proteins and repress
RT transcription of developmentally controlled E2F target genes.";
RL Cell 119:181-193(2004).
RN [7]
RP IDENTIFICATION IN THE DREAM COMPLEX.
RX PubMed=15545624; DOI=10.1101/gad.1255204;
RA Lewis P.W., Beall E.L., Fleischer T.C., Georlette D., Link A.J.,
RA Botchan M.R.;
RT "Identification of a Drosophila Myb-E2F2/RBF transcriptional repressor
RT complex.";
RL Genes Dev. 18:2929-2940(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381; SER-389; SER-396;
RP THR-445; THR-447; THR-557; SER-558; THR-566 AND SER-569, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: DNA-binding protein that specifically recognizes the sequence
CC 5'-YAAC[GT]G-3'. Component of the DREAM complex, a multiprotein complex
CC that can both act as a transcription activator or repressor depending
CC on the context. In follicle cells, the complex plays a central role in
CC the site-specific DNA replication at the chorion loci. During
CC development, the complex represses transcription of developmentally
CC controlled E2F target genes. {ECO:0000269|PubMed:12490953,
CC ECO:0000269|PubMed:15479636}.
CC -!- SUBUNIT: Component of the DREAM complex at least composed of Myb, Caf1-
CC 55, mip40, mip120, mip130, E2f2, Dp, Rbf, Rbf2, lin-52, HDAC1/Rpd3 and
CC l(3)mbt. {ECO:0000269|PubMed:12490953, ECO:0000269|PubMed:15479636,
CC ECO:0000269|PubMed:15545624}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X05939; CAA29373.1; -; mRNA.
DR EMBL; AE014298; AAF48529.1; -; Genomic_DNA.
DR EMBL; M11281; AAA70367.1; -; Genomic_DNA.
DR PIR; S00578; TVFFMA.
DR RefSeq; NP_511170.1; NM_078615.4.
DR RefSeq; NP_996454.1; NM_206731.2.
DR RefSeq; NP_996456.1; NM_206733.2.
DR RefSeq; NP_996457.1; NM_206734.2.
DR AlphaFoldDB; P04197; -.
DR SMR; P04197; -.
DR BioGRID; 58891; 38.
DR DIP; DIP-22816N; -.
DR IntAct; P04197; 18.
DR MINT; P04197; -.
DR STRING; 7227.FBpp0089402; -.
DR iPTMnet; P04197; -.
DR PaxDb; P04197; -.
DR DNASU; 32543; -.
DR EnsemblMetazoa; FBtr0074169; FBpp0073961; FBgn0002914.
DR EnsemblMetazoa; FBtr0074170; FBpp0089402; FBgn0002914.
DR EnsemblMetazoa; FBtr0074171; FBpp0089403; FBgn0002914.
DR EnsemblMetazoa; FBtr0074173; FBpp0089405; FBgn0002914.
DR GeneID; 32543; -.
DR KEGG; dme:Dmel_CG9045; -.
DR CTD; 4602; -.
DR FlyBase; FBgn0002914; Myb.
DR VEuPathDB; VectorBase:FBgn0002914; -.
DR eggNOG; KOG0048; Eukaryota.
DR HOGENOM; CLU_015440_4_1_1; -.
DR InParanoid; P04197; -.
DR OMA; WEIIGPH; -.
DR OrthoDB; 219341at2759; -.
DR PhylomeDB; P04197; -.
DR SignaLink; P04197; -.
DR BioGRID-ORCS; 32543; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32543; -.
DR PRO; PR:P04197; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0002914; Expressed in oviduct (Drosophila) and 28 other tissues.
DR ExpressionAtlas; P04197; differential.
DR Genevisible; P04197; DM.
DR GO; GO:0000791; C:euchromatin; IDA:FlyBase.
DR GO; GO:0031523; C:Myb complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0007099; P:centriole replication; IMP:FlyBase.
DR GO; GO:0007098; P:centrosome cycle; IMP:FlyBase.
DR GO; GO:0030261; P:chromosome condensation; IMP:FlyBase.
DR GO; GO:0007307; P:eggshell chorion gene amplification; IMP:FlyBase.
DR GO; GO:0007030; P:Golgi organization; IMP:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; IDA:FlyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:FlyBase.
DR GO; GO:0045792; P:negative regulation of cell size; IMP:FlyBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0090282; P:positive regulation of transcription involved in G2/M transition of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IDA:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007051; P:spindle organization; IMP:FlyBase.
DR CDD; cd00167; SANT; 3.
DR InterPro; IPR015395; C-myb_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF09316; Cmyb_C; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR SMART; SM00717; SANT; 3.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51294; HTH_MYB; 2.
PE 1: Evidence at protein level;
KW Activator; Chromosome; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..657
FT /note="Myb protein"
FT /id="PRO_0000197052"
FT DOMAIN 87..130
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 131..186
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 187..237
FT /note="HTH myb-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 159..182
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 210..233
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 445
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 447
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 557
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 566
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 370
FT /note="A -> V (in Ref. 1; CAA29373)"
FT /evidence="ECO:0000305"
FT CONFLICT 440..441
FT /note="QL -> KY (in Ref. 4; AAA70367)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 657 AA; 74045 MW; 8265B37ABB250AE4 CRC64;
MASASTENGE ELMNYGSNSD SEESEYSENE DTQVCDKDSQ QNSNADSGYP LDSPELQDSK
TTGQKGQNKS GKTSIGAVHP NYGFGKRWSK SEDVLLKQLV ETHGENWEII GPHFKDRLEQ
QVQQRWAKVL NPELIKGPWT RDEDDMVIKL VRNFGPKKWT LIARYLNGRI GKQCRERWHN
HLNPNIKKTA WTEKEDEIIY QAHLELGNQW AKIAKRLPGR TDNAIKNHWN STMRRKYDVE
RRSVNASGSD LKSSRTHLIT LIKSGGISKC MNNMQHNKES GGEAVNKSEN ADGASVTAVK
GGDLAQESQD DHQKGSNLAH LSMQHLIKLT MPRQTPIILK RTRKHIPETH HQAGCSSSET
FNQEEAAGNA RSRPPSSPVI SPIKSLPFSP SHFLKSPCLT TFEDMDLRAS TPVTKVYNRV
GMEIKKEMET SSIETPHKSQ LGPRTPTPFK KALAAIGKKR DGRRYEPSSP SSLVEDLAEI
IHEEHLSNSL TANNSKMMGA ADQNSTLSTE YNAQSPPHMK RARKSLLSTW SSNHPYNAGS
AKRIQPFETE TPSKFLTSPG DILKDTLCSE QDLPFDEGRK ENRPFHNRRI NKYRGGLTYD
HVIDPKWARV ACGKSRDQMF MEEQAYACLK NLSCISRSLN FEKQKCLVNS FDRFGSL
