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MED30_DROME
ID   MED30_DROME             Reviewed;         318 AA.
AC   Q9W0P3;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 30;
DE   AltName: Full=Mediator complex subunit 30;
DE   AltName: Full=dMED20;
DE   AltName: Full=dTRAP25;
GN   Name=MED30; Synonyms=Trap25; ORFNames=CG17183;
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.
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].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR
RP   COMPLEX, FUNCTION OF THE MEDIATOR COMPLEX, AND INTERACTION WITH MED6 AND
RP   MED17.
RX   PubMed=12021283; DOI=10.1074/jbc.m204144200;
RA   Gu J.-Y., Park J.M., Song E.J., Mizuguchi G., Yoon J.H., Kim-Ha J.,
RA   Lee K.-J., Kim Y.-J.;
RT   "Novel Mediator proteins of the small Mediator complex in Drosophila SL2
RT   cells.";
RL   J. Biol. Chem. 277:27154-27161(2002).
CC   -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC       the regulated transcription of nearly all RNA polymerase II-dependent
CC       genes. Mediator functions as a bridge to convey information from gene-
CC       specific regulatory proteins to the basal RNA polymerase II
CC       transcription machinery. Mediator is recruited to promoters by direct
CC       interactions with regulatory proteins and serves as a scaffold for the
CC       assembly of a functional preinitiation complex with RNA polymerase II
CC       and the general transcription factors. {ECO:0000269|PubMed:12021283}.
CC   -!- SUBUNIT: Component of the Mediator complex, which includes at least
CC       CDK8, MED4, MED6, MED11, MED14, MED17, MED18, MED20, MED21, MED22,
CC       MED27, MED28, MED30 and MED31. {ECO:0000269|PubMed:12021283}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 30 family.
CC       {ECO:0000305}.
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DR   EMBL; AE014296; AAF47400.1; -; Genomic_DNA.
DR   EMBL; AY061627; AAL29175.1; -; mRNA.
DR   RefSeq; NP_612046.1; NM_138202.4.
DR   AlphaFoldDB; Q9W0P3; -.
DR   SMR; Q9W0P3; -.
DR   BioGRID; 63633; 34.
DR   DIP; DIP-22594N; -.
DR   IntAct; Q9W0P3; 5.
DR   STRING; 7227.FBpp0072457; -.
DR   PaxDb; Q9W0P3; -.
DR   PRIDE; Q9W0P3; -.
DR   DNASU; 38078; -.
DR   EnsemblMetazoa; FBtr0072558; FBpp0072457; FBgn0035149.
DR   GeneID; 38078; -.
DR   KEGG; dme:Dmel_CG17183; -.
DR   CTD; 90390; -.
DR   FlyBase; FBgn0035149; MED30.
DR   VEuPathDB; VectorBase:FBgn0035149; -.
DR   eggNOG; ENOG502QV3C; Eukaryota.
DR   GeneTree; ENSGT00390000010887; -.
DR   HOGENOM; CLU_074190_0_0_1; -.
DR   InParanoid; Q9W0P3; -.
DR   OMA; YFRTIRL; -.
DR   OrthoDB; 1549016at2759; -.
DR   PhylomeDB; Q9W0P3; -.
DR   BioGRID-ORCS; 38078; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 38078; -.
DR   PRO; PR:Q9W0P3; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0035149; Expressed in secondary oocyte and 21 other tissues.
DR   Genevisible; Q9W0P3; DM.
DR   GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   InterPro; IPR021019; Mediator_Med30_met.
DR   PANTHER; PTHR31705; PTHR31705; 1.
DR   Pfam; PF11315; Med30; 1.
PE   1: Evidence at protein level;
KW   Activator; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..318
FT                   /note="Mediator of RNA polymerase II transcription subunit
FT                   30"
FT                   /id="PRO_0000305910"
FT   REGION          1..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   318 AA;  35301 MW;  E8D4E59A00E65DF5 CRC64;
     MWKYGQNQGN QGPSSGGGGG GGPNMMPMGG FGMQHGNMQQ MHMSPQHQQQ QQQMGMMGGP
     GSMQMNPQGP GGPGGLMPGM SPQHQMQQQQ QQQMMQQQMM VPQQGVGVGV GMGGGVGMGG
     GGVVPQQQQQ QPQQNMPQQN IPQQQQQLNP VAGIPPGGAG GSNNMLAISQ QNPHKEINIV
     QLSRLGQETV QDIASRFQEV FASLKGIQPT SHRENSSEKK VQEYFRTIRL LFKRVRIIYE
     KCNDAGMDYM SAESLIPYRD EPEPRIEPSL CDEYRKVLQE NHELIETVKL KNRQLREIID
     RTRIIIWEIN TMLAMRRS
 
 
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