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MED12_DROME
ID   MED12_DROME             Reviewed;        2531 AA.
AC   Q9VW47; Q8MQW4; Q9GPH4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 12;
DE   AltName: Full=Mediator complex subunit 12;
DE   AltName: Full=Mediator complex subunit Kohtalo;
DE   AltName: Full=dTRAP230;
GN   Name=kto; Synonyms=Med12, Trap230; ORFNames=CG8491;
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], AND FUNCTION.
RX   PubMed=11171343; DOI=10.1242/dev.128.4.603;
RA   Treisman J.E.;
RT   "Drosophila homologues of the transcriptional coactivation complex subunits
RT   TRAP240 and TRAP230 are required for identical processes in eye-antennal
RT   disc development.";
RL   Development 128:603-615(2001).
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] OF 964-2531.
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   [5]
RP   FUNCTION, INTERACTION WITH SKD, AND SUBCELLULAR LOCATION.
RX   PubMed=12835386; DOI=10.1242/dev.00607;
RA   Janody F., Martirosyan Z., Benlali A., Treisman J.E.;
RT   "Two subunits of the Drosophila mediator complex act together to control
RT   cell affinity.";
RL   Development 130:3691-3701(2003).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH CYCC; CDK8 AND SKD.
RX   PubMed=17290221; DOI=10.1038/sj.emboj.7601566;
RA   Loncle N., Boube M., Joulia L., Boschiero C., Werner M., Cribbs D.L.,
RA   Bourbon H.-M.;
RT   "Distinct roles for Mediator Cdk8 module subunits in Drosophila
RT   development.";
RL   EMBO J. 26:1045-1054(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-781, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=17372656; DOI=10.1039/b617545g;
RA   Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA   Eng J.K., Aebersold R., Tao W.A.;
RT   "An integrated chemical, mass spectrometric and computational strategy for
RT   (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT   Kc167 cells.";
RL   Mol. Biosyst. 3:275-286(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-745; SER-748; SER-806;
RP   SER-1356 AND THR-1360, 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       regulated gene 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. Required for leg and eye
CC       development and macrochaete specification or differentiation.
CC       {ECO:0000269|PubMed:11171343, ECO:0000269|PubMed:12835386,
CC       ECO:0000269|PubMed:17290221}.
CC   -!- SUBUNIT: Component of the Cdk8 module of the Mediator complex, composed
CC       of CycC, Cdk8, kto and skd.
CC   -!- INTERACTION:
CC       Q9VW47; P25008: CycC; NbExp=2; IntAct=EBI-139710, EBI-195485;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12835386}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 12 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM52769.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF324426; AAG48328.1; -; mRNA.
DR   EMBL; AE014296; AAF49103.2; -; Genomic_DNA.
DR   EMBL; AY122257; AAM52769.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_524786.1; NM_080047.2.
DR   AlphaFoldDB; Q9VW47; -.
DR   BioGRID; 69311; 14.
DR   DIP; DIP-29990N; -.
DR   IntAct; Q9VW47; 9.
DR   MINT; Q9VW47; -.
DR   STRING; 7227.FBpp0074653; -.
DR   iPTMnet; Q9VW47; -.
DR   PaxDb; Q9VW47; -.
DR   PRIDE; Q9VW47; -.
DR   EnsemblMetazoa; FBtr0074884; FBpp0074653; FBgn0001324.
DR   GeneID; 44830; -.
DR   KEGG; dme:Dmel_CG8491; -.
DR   CTD; 44830; -.
DR   FlyBase; FBgn0001324; kto.
DR   VEuPathDB; VectorBase:FBgn0001324; -.
DR   eggNOG; KOG3598; Eukaryota.
DR   GeneTree; ENSGT00440000037505; -.
DR   HOGENOM; CLU_000904_0_0_1; -.
DR   InParanoid; Q9VW47; -.
DR   OMA; YQQSHDK; -.
DR   OrthoDB; 20034at2759; -.
DR   PhylomeDB; Q9VW47; -.
DR   SignaLink; Q9VW47; -.
DR   BioGRID-ORCS; 44830; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; kto; fly.
DR   GenomeRNAi; 44830; -.
DR   PRO; PR:Q9VW47; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0001324; Expressed in second segment of antenna (Drosophila) and 23 other tissues.
DR   ExpressionAtlas; Q9VW47; baseline and differential.
DR   Genevisible; Q9VW47; DM.
DR   GO; GO:0070847; C:core mediator complex; IPI:FlyBase.
DR   GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
DR   GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR   GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB.
DR   GO; GO:0022416; P:chaeta development; IMP:FlyBase.
DR   GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR   GO; GO:0035072; P:ecdysone-mediated induction of salivary gland cell autophagic cell death; IMP:FlyBase.
DR   GO; GO:0036011; P:imaginal disc-derived leg segmentation; IMP:FlyBase.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:FlyBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0045498; P:sex comb development; IMP:FlyBase.
DR   InterPro; IPR019035; Mediator_Med12.
DR   InterPro; IPR021990; Mediator_Med12_LCEWAV.
DR   Pfam; PF09497; Med12; 1.
DR   Pfam; PF12145; Med12-LCEWAV; 1.
DR   SMART; SM01281; Med12; 1.
PE   1: Evidence at protein level;
KW   Activator; Developmental protein; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..2531
FT                   /note="Mediator of RNA polymerase II transcription subunit
FT                   12"
FT                   /id="PRO_0000312963"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          584..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          742..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          796..824
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1585..1608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1898..2092
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2114..2218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2469..2508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1936..2054
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2066..2092
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2114..2209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         745
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         748
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         781
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17372656"
FT   MOD_RES         806
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1356
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1360
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
SQ   SEQUENCE   2531 AA;  279499 MW;  68B0CD469E83A9F5 CRC64;
     MLSMLQEKRP LKRTRLGPPD IYPQDAKQRE DELTPTNVKH GFTTTPPLSD EFGTAHNSNV
     NASKVSAFFS GVLAKKEELM TLPDTGRKKQ QINCKDNFWP VSPRRKCTVD AWFKDLAGNK
     PLLSLAKRAP SFNKKEEIFI TLCENQVNMQ RATWFIKLSA AYTLSFTESK NKKRSIYDPA
     AEWTGNMIKF MKELLPKLQE YYQQNHDKSS SNGTTSGSLT AAGNGPASNG STGTSSINSV
     TGSSASTNVI PVPSMASPLP PIHSPANGQQ AAPGGGVNAG SVMPTTGSLG GVVGGPGSSV
     VGGAAGAGAA VPPGSTISGI GSQFEDSRNA LKYWKYCHQL SKYMYEESLL DRQEFLNWIL
     DLLDKMRTQA SFDEPLKKLV LSFALQYMHD FVQSERLCRK MAYIVSKKLA QLLNTVVEQQ
     TIKELDEPKL QQDPYELALQ EQMSCPHHRD IVLYLSTILQ IITIECPTAL VWSGIAAHRA
     PSSLLGSPLD HLPLAPSVLP MPTRCPRTNH EIRRQLRAAE SDIVLRTQHA EQRWFAAKWL
     SAGKNQYTSV LATLDHLDTH CFDRMEHNNS IDTLYAQIFP SPTVSRRREE DQVEPRPPYE
     PKQDKDTVRI LCEWAVSGQR WGEHRAMVVA ILLDKRQIDV TSTPADQQSS DKDDKDSLAS
     GAGLIDGLPV FQHVLMHFLD HDAPVLDEHV SSPQQRTEFT NLVQLFSALI RHDVFSHNAY
     MHTLISRGDL LLESVLVIKS GTTATKTSPP PPAPPPTTTH GFDDDGFGGG LDFKHNEFDD
     SNVDDDLDKL VQNIKEKGQQ HEAPDSPKIG PPGDGETNPG GSISRHYVYT KHFPIPQDDP
     SMSSYSSESN QRYILLFGVG KERDEKKHAV KKMSKEIGKL FTKKFSIDVA AAGHVKKHSR
     NEFNFEATTS KCQQMAYFDQ HVVTAQCAAN VLEQLNGFAL GNNNYLPVQE HVAFLFDLME
     LALNIYSLLE LCDSLLKELP EVEHQLQLKK SNLVRSYTTS LALYIVSILR RYHSCLLLSP
     EQTLSVFEGV CRTIRHVSNP SECTSAERCI IAYLSDLHES CVLLQGKEQS TEYYQQLQCI
     KRFKDIFNTP EQLDLPPQGY NPLLLQELFM APRRGGKLDP HWLGTLHESP ANVYSFVSNA
     LIAVCRETDN ERLNDVALAC AELTASCNVL SEEWIYALQS LCSGSKSPRY PHLGGQVDIG
     QLKTHNALAV FVCILVARHC FSLADFVSKF ALPTLARSVS AGGAELSVDA EAGARLTCHL
     VLKLFKTLEI PQPGMYSVST SPNPLHAVGN DFSIRLSCDR HLLVGAHKTI PIAAVLAVLK
     AILIVVDNAA LKTPLASGSG TSSGGLGGAF GSGKRSGFNT PVHPGSTPKS NEQRPADLSQ
     ILGTSDLQLG SSLTSEPEAL QQPSVGGMEQ ISLLEFAQAV LKQICAQEHV LERCLKNAEQ
     LCDMIIDEML TAKQAQRVLH MICYPEPEFN IISELDQRSM IVRILENLGQ WTLRISWLDL
     QLMYRQSLSN NAELNVWLDT VARAAIDVFH MEEVVLPGAV KATHKPKPST WLVAPLIAKL
     TPAVQGRILR VAGQVLESMN YFSKVSKSDC NSSGSGDERE KSNSCHSSNS YGLGGVPARN
     KKMPLDYQPF LGLILTCLKG QDEYKENLLV SLYAQLSQCL QSFAELDTIG GIDEPQAREE
     ILDALQLRFS LVGGMFEAIQ KNSTPTTDWA ILLAQLVCQG VVDLSCNREL FTTVVDMLAT
     LVHSTLVSDD ERHYMNLMKK LKKEIGEKNN ASIRVIRQLL PLYKQPTEVI ACEHSGMDTK
     GNKICDIDKK QLRISDKQRI SVWDILEGHK NPAPLSWVWF GAVKLERKPL TYEEAHRNLK
     YHTHSLVKPS SYYYEPLPLP PEDIEPVPEK ICIKDEMKAD TPSSVDQSPS AVVGGTGRGR
     GKGTTTRKRK PKNPKTPPVV NTQQQQPQLA QQPQQPQNVQ QQQLQQQQQQ QQHMQQQHMQ
     QQQMQPNQMG QMPMNMPMNM QQFAPNPNNM MQQNAMLQQQ QQQQMQQMGN NPMQQQLNVG
     GGNGQPNPQM NFMQQGPGGG GAGPQGMPGQ QQQWHNAPQQ QQPPQPYHNQ YAPHQQNMQS
     NRIERPPLNA NSKQALSQML RQRQPFQQQA QQGPGGGFNP MQQQPQASQQ QPGPQQQMNP
     NQMRQQQMNP QQNPQSVAAF NAMQQQPQQN AQQQQMNPNQ QQQQQFMRGG NMRPGMAPNQ
     MNQMNMGGQG MSQNPMMQQQ IPQNMVGMVN PNANQMMQSG GAQGGNGVGV GVGVGVGGAG
     NNPNMGMGGM PQQGMIQQQP QQQPQQQVQF QNFQNQYQQQ QQQGMQQQGG GAGVGVGVGM
     APNQQQQQQA NMMGNFNPQM QQGNRNNPDF MAAAAVAQQQ QQQQQQQRVV PGGMMAGNRN
     QYMNQAPNVT MSTMMGPGPG GVVGQVPPYA RQQSAGGGKP GVLNTQQQFQ QQQQQQQQLR
     HQMMQLQGMG GGAGGGMGAG PQQGGGAVGG GAGGGMVPQQ QSMNQQQTPN LVAQLQRQNM
     MGQQQYQPPP Y
 
 
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