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MED1_DROME
ID   MED1_DROME              Reviewed;        1475 AA.
AC   Q9VP05; B5RJH3; Q9GYW7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 1;
DE   AltName: Full=Mediator complex subunit 1;
DE   AltName: Full=dTRAP220;
GN   Name=MED1; Synonyms=Trap220; ORFNames=CG7162;
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].
RA   Southworth J.W., Kennison J.A.;
RT   "Transcriptional coactivators in Drosophila.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
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 [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RA   Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION.
RX   PubMed=16751183; DOI=10.1101/gad.1418806;
RA   Marr M.T. II, Isogai Y., Wright K.J., Tjian R.;
RT   "Coactivator cross-talk specifies transcriptional output.";
RL   Genes Dev. 20:1458-1469(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-830; SER-834; SER-854 AND
RP   SER-858, AND IDENTIFICATION 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: 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 (By similarity). Required for
CC       activated transcription of the MtnA, MtnB and MtnD genes. {ECO:0000250,
CC       ECO:0000269|PubMed:16751183}.
CC   -!- SUBUNIT: Component of the Mediator complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AF289996; AAG02461.1; -; mRNA.
DR   EMBL; AE014296; AAF51757.2; -; Genomic_DNA.
DR   EMBL; BT044447; ACH92512.1; -; mRNA.
DR   RefSeq; NP_649341.1; NM_141084.3.
DR   AlphaFoldDB; Q9VP05; -.
DR   BioGRID; 65647; 11.
DR   IntAct; Q9VP05; 3.
DR   STRING; 7227.FBpp0078118; -.
DR   iPTMnet; Q9VP05; -.
DR   PaxDb; Q9VP05; -.
DR   PRIDE; Q9VP05; -.
DR   DNASU; 40403; -.
DR   EnsemblMetazoa; FBtr0078464; FBpp0078118; FBgn0037109.
DR   GeneID; 40403; -.
DR   KEGG; dme:Dmel_CG7162; -.
DR   CTD; 5469; -.
DR   FlyBase; FBgn0037109; MED1.
DR   VEuPathDB; VectorBase:FBgn0037109; -.
DR   eggNOG; ENOG502QPZ7; Eukaryota.
DR   GeneTree; ENSGT00660000095569; -.
DR   InParanoid; Q9VP05; -.
DR   OMA; HAMKLTY; -.
DR   OrthoDB; 182447at2759; -.
DR   PhylomeDB; Q9VP05; -.
DR   Reactome; R-DME-383280; Nuclear Receptor transcription pathway.
DR   Reactome; R-DME-400206; Regulation of lipid metabolism by PPARalpha.
DR   Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR   Reactome; R-DME-9707564; Cytoprotection by HMOX1.
DR   SignaLink; Q9VP05; -.
DR   BioGRID-ORCS; 40403; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; MED1; fly.
DR   GenomeRNAi; 40403; -.
DR   PRO; PR:Q9VP05; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0037109; Expressed in cleaving embryo and 22 other tissues.
DR   ExpressionAtlas; Q9VP05; baseline and differential.
DR   Genevisible; Q9VP05; DM.
DR   GO; GO:0016592; C:mediator complex; IMP:FlyBase.
DR   GO; GO:0005634; C:nucleus; IC:FlyBase.
DR   GO; GO:0003712; F:transcription coregulator activity; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:FlyBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR   InterPro; IPR019680; Mediator_Med1.
DR   Pfam; PF10744; Med1; 1.
PE   1: Evidence at protein level;
KW   Activator; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1475
FT                   /note="Mediator of RNA polymerase II transcription subunit
FT                   1"
FT                   /id="PRO_0000302023"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          616..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          709..992
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1135..1166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1184..1245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1263..1354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1387..1475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..642
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        709..730
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        753..782
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        783..801
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        856..936
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        956..990
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1184..1232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1263..1299
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1311..1345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1387..1426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1444..1460
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         830
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         834
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         854
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         858
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
SQ   SEQUENCE   1475 AA;  149531 MW;  273E6CB3949DC6CE CRC64;
     MSGSNAKSSG TGFGSHIPSI EEKNKQIQQE TMMEKLRAKY RNKPKSYEEI KKSVRMYFIE
     KHYPLDPLCK ATLQSALDKL QHYIKVTSRH GLVERLESLS RQLGLKFMED QQLLFISTDM
     FYVEILLDAA GSLSDVKVHH ECKIEQQSSE LVACLKSGDF ADFTVQLEGL SSIYQLNAEP
     KVKKKAFVAL QAMETDIQSL YQLHLQGHSG DSYSLMTSSS VGLVLPRRGG HPMRLTYFCP
     PLHLPEGDPK LASGDFTIDQ VMRSSYGLSA TINLEGSSAN KLQTLPTVTL VRDAQTGLEV
     PTYAQLNQNN SLLMPATFVL RLNKPMPVCL ESLKALGLPG LDSVATPPGP PTTVLNLIVQ
     TASKQAIKNT QRGLYVNLPK ETHCYFFTDN RKLQGTLVSS LPFTEPAQVP RIVAFLKKQA
     LFYTLLASCV REQQKQYNDM DSTVILEVTA VSFNQITVEL QHPYEESLAT VDFLLEDGQP
     TCSVYCLTNE YELLSQKLTR TARKVVSIPM VIYKLLKCWD EEHEFKLHGA IGPGSGSGAI
     GGGGMSGGGP VSGVGNNFSQ FSMDTPTPSD GSLPGGGFAN INNLKMDAKS RSLADAFAAS
     TSAAAAIAGL INLKRETDPQ SGSSASGTTV SGSSSSSGSA KTSDHDIADK YKNIWKDKTP
     NLKHCVSITP IPGDGKSGSA GGVSGVEVQR TGGIEIIPLN AQAAIAGGGV TASSSATPTT
     ITITPITGKD PSKDSTKKST AASAGVGVAA KRPHESSTSS SSTSGCSGSG SSMSSSASSG
     SSDTQKEKKR KKKRDDSPMG PPEKIYSRQN SPAGGADASA TGGVVRKFSS PSSSPKAGGG
     GQGLMAGVPT ARPSPKHSPV YSSPKHNTAS NSPKSPFGTH SPKHGSSGKP SMSTLKSAAT
     AATILSPKGD KSSSAVGNTS SGPSASSGSS GATGLVRSFA SVGAPPPPPP IPPLASSSGS
     ISSSQSLKKE KTSSASGSSS TSSSATAGVA SGGGISPASV AAAVAALKSS QQQMKSVASL
     SHLAAGGGLG SYAAPSGAGA SGAAAVVVGA GAGAGAGASG LELSALRKGM AGGAVSLMTS
     TAALAPTIPA PTTTVAAGSA ASLVSPVSAV VGQGQETAGA AAAATLATAT ILQQQPQPGA
     APTSSCLTTS GGSSDSAGSI NPAGASTEYM VKPSSQEGLK LTINKTGSSK SSGTGSGSSS
     SSGLQAKAKS SSSGATSFAG STGSTKKQHT GLKPGVNSGP ASKKATAAVS SATASSSKHF
     FQKANSSGNL SSKLSGSGSG GGIPLTKSNS TNSFQEHNAP RRRPSMGALA SGSSGGGSGQ
     RKLGSASGGG SGSSGSVSPA LSGSMSQPPP RFDHHTDMMT ILQYASPTMA ASMEGFIKGL
     HNKFQIPKLS QRGSGGNTTS GRSTPSGSSE PALAGTSSSI LGPIASSTGL TEPEAKPPVP
     PSQSGNEGLL NLSSTAGTPS ADGIDEELLA SLAGE
 
 
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