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TFDP_DROME
ID   TFDP_DROME              Reviewed;         445 AA.
AC   Q24318; B8A3X4; O17472; O44080; Q86PE0; Q8ML56; Q9V6M0;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   03-AUG-2022, entry version 180.
DE   RecName: Full=Transcription factor Dp;
GN   Name=Dp; ORFNames=CG4654;
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 [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   [2]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Booth B.,
RA   Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA   George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA   Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA   Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA   Celniker S.E.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 50-445.
RC   TISSUE=Eye imaginal disk;
RX   PubMed=8022787; DOI=10.1073/pnas.91.14.6359;
RA   Dynlacht B.D., Brook A., Dembski M., Yenush L., Dyson N.;
RT   "DNA-binding and trans-activation properties of Drosophila E2F and DP
RT   proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:6359-6363(1994).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 83-445.
RX   PubMed=9271122; DOI=10.1101/gad.11.15.1999;
RA   Royzman I., Whittaker A.J., Orr-Weaver T.L.;
RT   "Mutations in Drosophila DP and E2F distinguish G1-S progression from an
RT   associated transcriptional program.";
RL   Genes Dev. 11:1999-2011(1997).
RN   [7]
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   [8]
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND IDENTIFICATION BY
RP   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: Component of the DREAM complex, a multiprotein complex that
CC       can both act as a transcription activator or repressor depending on the
CC       context. In follicle cells, the complex plays a central role in the
CC       site-specific DNA replication at the chorion loci. During development,
CC       the complex represses transcription of developmentally controlled E2F
CC       target genes. Can stimulate E2F-dependent transcription.
CC       {ECO:0000269|PubMed:15479636}.
CC   -!- SUBUNIT: Heterodimer of E2f and Dp. Cooperate to give sequence-specific
CC       DNA binding and optimal trans-activation. Component of the DREAM
CC       complex at least composed of Myb, Caf1-55, mip40, mip120, mip130, E2f2,
CC       Dp, Rbf, Rbf2, lin-52, HDAC1/Rpd3 and l(3)mbt.
CC       {ECO:0000269|PubMed:15479636, ECO:0000269|PubMed:15545624}.
CC   -!- INTERACTION:
CC       Q24318; Q24472: Rbf; NbExp=3; IntAct=EBI-530830, EBI-145741;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=Q24318-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=Q24318-2; Sequence=VSP_014146;
CC   -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
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DR   EMBL; AE013599; AAF58403.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAM68602.1; -; Genomic_DNA.
DR   EMBL; AY069526; AAL39671.1; -; mRNA.
DR   EMBL; BT003183; AAO24938.1; -; mRNA.
DR   EMBL; BT056266; ACL68713.1; -; mRNA.
DR   EMBL; X79708; CAA56147.2; -; mRNA.
DR   EMBL; AF011362; AAB87765.1; -; Genomic_DNA.
DR   PIR; B55745; B55745.
DR   RefSeq; NP_477039.1; NM_057691.4. [Q24318-1]
DR   RefSeq; NP_725267.1; NM_165974.3. [Q24318-2]
DR   AlphaFoldDB; Q24318; -.
DR   SMR; Q24318; -.
DR   BioGRID; 62224; 31.
DR   IntAct; Q24318; 11.
DR   STRING; 7227.FBpp0086853; -.
DR   iPTMnet; Q24318; -.
DR   PaxDb; Q24318; -.
DR   PRIDE; Q24318; -.
DR   DNASU; 36461; -.
DR   EnsemblMetazoa; FBtr0087740; FBpp0086853; FBgn0011763. [Q24318-1]
DR   EnsemblMetazoa; FBtr0087741; FBpp0086854; FBgn0011763. [Q24318-2]
DR   GeneID; 36461; -.
DR   KEGG; dme:Dmel_CG4654; -.
DR   CTD; 13450; -.
DR   FlyBase; FBgn0011763; Dp.
DR   VEuPathDB; VectorBase:FBgn0011763; -.
DR   eggNOG; KOG2829; Eukaryota.
DR   GeneTree; ENSGT00940000169233; -.
DR   InParanoid; Q24318; -.
DR   OMA; NNPMKIK; -.
DR   PhylomeDB; Q24318; -.
DR   Reactome; R-DME-1538133; G0 and Early G1.
DR   Reactome; R-DME-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR   Reactome; R-DME-69231; Cyclin D associated events in G1.
DR   Reactome; R-DME-8953750; Transcriptional Regulation by E2F6.
DR   BioGRID-ORCS; 36461; 1 hit in 3 CRISPR screens.
DR   ChiTaRS; Dp; fly.
DR   GenomeRNAi; 36461; -.
DR   PRO; PR:Q24318; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0011763; Expressed in oocyte and 53 other tissues.
DR   ExpressionAtlas; Q24318; baseline and differential.
DR   Genevisible; Q24318; DM.
DR   GO; GO:0031523; C:Myb complex; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR   GO; GO:0035189; C:Rb-E2F complex; IDA:FlyBase.
DR   GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR   GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR   GO; GO:0008069; P:dorsal/ventral axis specification, ovarian follicular epithelium; IMP:FlyBase.
DR   GO; GO:0007307; P:eggshell chorion gene amplification; TAS:FlyBase.
DR   GO; GO:0007113; P:endomitotic cell cycle; TAS:FlyBase.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:FlyBase.
DR   GO; GO:0045476; P:nurse cell apoptotic process; TAS:FlyBase.
DR   GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:FlyBase.
DR   GO; GO:0045850; P:positive regulation of nurse cell apoptotic process; IMP:FlyBase.
DR   GO; GO:0051726; P:regulation of cell cycle; IMP:FlyBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd14458; DP_DD; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.20.140.80; -; 1.
DR   InterPro; IPR037241; E2F-DP_heterodim.
DR   InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
DR   InterPro; IPR038168; TF_DP_C_sf.
DR   InterPro; IPR014889; Transc_factor_DP_C.
DR   InterPro; IPR015648; Transcrpt_fac_DP.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR12548; PTHR12548; 1.
DR   Pfam; PF08781; DP; 1.
DR   Pfam; PF02319; E2F_TDP; 1.
DR   PIRSF; PIRSF009404; Transcription_factor_DP; 1.
DR   SMART; SM01138; DP; 1.
DR   SMART; SM01372; E2F_TDP; 1.
DR   SUPFAM; SSF144074; SSF144074; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..445
FT                   /note="Transcription factor Dp"
FT                   /id="PRO_0000219479"
FT   REGION          145..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          392..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         398
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   VAR_SEQ         1..22
FT                   /note="MAHSTGGTVKTDEVNFFFRNEH -> MCISETKEPPHLPISNSA (in
FT                   isoform B)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_014146"
FT   CONFLICT        117
FT                   /note="D -> G (in Ref. 4; AAO24938)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        343
FT                   /note="H -> L (in Ref. 6; AAB87765)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   445 AA;  49750 MW;  87F4DBB26CFE4E42 CRC64;
     MAHSTGGTVK TDEVNFFFRN EHGQISKMLK PAQNKSEMEG GKPVAVVYAT GSSARNSGSA
     SGIGNVGRMG AFSQMGSQGQ FIRLQDNGLS IPKTEAGTTY TTVSAQKTSG AGSGHYDLPL
     KGDRYVKFTP NPIKMKSKLH AIQSNSLHSM SASSSSVQRK RKPDKAGKGL RHFSMKVCEK
     VEEKGKTTYN EVADDLVSEE MKNNAYDNNC DQKNIRRRVY DALNVLMAIN VISKDKKEIR
     WIGLPANSTE TFLALEEENC QRRERIKQKN EMLREMIMQH VAFKGLVERN KRNESQGVVP
     SPNASIQLPF IIVNTHKSTK INCSVTNDKS EYIFKFDKTF EMHDDIEVLK RMGFLLGLDK
     GECTPENIER VKSWVPPNLA KYVEAYGTGK TGENMYESDD EDNEFNGYLE SANESQGFAQ
     HSAQHTTDGE FKLEMDDDEL DDDID
 
 
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