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MED15_CANGA
ID   MED15_CANGA             Reviewed;        1095 AA.
AC   Q6FRS9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 15;
DE   AltName: Full=Mediator complex subunit 15;
DE   AltName: Full=Transcription regulatory protein GAL11;
GN   Name=GAL11; Synonyms=MED15; OrderedLocusNames=CAGL0H06215g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the Mediator complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 15 family.
CC       {ECO:0000305}.
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DR   EMBL; CR380954; CAG59998.1; -; Genomic_DNA.
DR   RefSeq; XP_447065.1; XM_447065.1.
DR   PDB; 4D7X; NMR; -; A=1-86.
DR   PDBsum; 4D7X; -.
DR   AlphaFoldDB; Q6FRS9; -.
DR   BMRB; Q6FRS9; -.
DR   SMR; Q6FRS9; -.
DR   DIP; DIP-59822N; -.
DR   IntAct; Q6FRS9; 1.
DR   STRING; 5478.XP_447065.1; -.
DR   BindingDB; Q6FRS9; -.
DR   ChEMBL; CHEMBL4295608; -.
DR   PRIDE; Q6FRS9; -.
DR   EnsemblFungi; CAG59998; CAG59998; CAGL0H06215g.
DR   GeneID; 2888816; -.
DR   KEGG; cgr:CAGL0H06215g; -.
DR   CGD; CAL0131746; GAL11A.
DR   VEuPathDB; FungiDB:CAGL0H06215g; -.
DR   eggNOG; ENOG502QVXD; Eukaryota.
DR   HOGENOM; CLU_009962_0_0_1; -.
DR   InParanoid; Q6FRS9; -.
DR   OMA; KYWESMK; -.
DR   Proteomes; UP000002428; Chromosome H.
DR   GO; GO:0070847; C:core mediator complex; IEA:EnsemblFungi.
DR   GO; GO:0016592; C:mediator complex; IEA:InterPro.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:EnsemblFungi.
DR   GO; GO:0001095; F:TFIIE-class transcription factor complex binding; IEA:EnsemblFungi.
DR   GO; GO:0001097; F:TFIIH-class transcription factor complex binding; IEA:EnsemblFungi.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:EnsemblFungi.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:2000219; P:positive regulation of invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR   GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR   GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR   GO; GO:0070202; P:regulation of establishment of protein localization to chromosome; IEA:EnsemblFungi.
DR   GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IEA:EnsemblFungi.
DR   CDD; cd12191; gal11_coact; 1.
DR   Gene3D; 1.10.246.20; -; 1.
DR   InterPro; IPR033789; Gal11_coact.
DR   InterPro; IPR036529; KIX_dom_sf.
DR   InterPro; IPR036546; MED15_KIX.
DR   InterPro; IPR008626; Mediator_Med15_fun.
DR   Pfam; PF18535; Gal11_ABD1; 1.
DR   Pfam; PF16987; KIX_2; 1.
DR   Pfam; PF05397; Med15_fungi; 1.
DR   SUPFAM; SSF47040; SSF47040; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1095
FT                   /note="Mediator of RNA polymerase II transcription subunit
FT                   15"
FT                   /id="PRO_0000304671"
FT   REGION          66..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          265..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          633..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          737..847
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1050..1075
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..84
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        748..847
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1050..1066
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           2..5
FT                   /evidence="ECO:0007829|PDB:4D7X"
FT   HELIX           9..29
FT                   /evidence="ECO:0007829|PDB:4D7X"
FT   HELIX           34..52
FT                   /evidence="ECO:0007829|PDB:4D7X"
FT   HELIX           58..84
FT                   /evidence="ECO:0007829|PDB:4D7X"
SQ   SEQUENCE   1095 AA;  121152 MW;  903F3DF1ADC85348 CRC64;
     MSSKETIPMH QRSQNVAELL TVLMDINKIN GGDSTTAEKM KVHAKSFEAA LFEKSSSKEE
     YQKTMKSKID AMRSTRDKRK RESVGSASMM ANLGQDGTNN NNNNNNNNNN NLNMAASFMG
     GDMFGRNQSP AQNSNANTNL NTNVGPGVNG PNGNDGTANP QMFMNQQAQA RQQAAARQLK
     NRQMGGSSAQ QQQLTQQQQQ LLNQMRVAPI PKELLQRIPN LPPGVTTWEQ VTALAQQNRL
     SAQDMSIAKD IYKIHQQYLI KAKLQQQQQR QQQQRQQGNP DVNNNMAGSN NNNNNNLPMA
     QQQMQQRQQQ QQQSQQQQNR NPNQRHNVLS QINQMFTADE QRALLQEAME ACKNFQKTHF
     GGQMSDANKQ AFIKKFINSK ALKKLEAMRM AQGGNNNANL NKGQADMLQR QQANMQMNQQ
     QQRAAQNQRR GPVMNDAVSQ GYNNQMNSAA DSTMNNSNQP MNIGNNGVNM IPNQSQQQQQ
     TNRPKEQTPQ QPQQRIQSNR SVPMLNPTPE DVEVVRRISA EAAKTQLRLT DLTNSLTPQE
     RDEIKKRLQK NQQLFAQVSS YAPQVYLFTK SESFLKEVLQ LRIFIKEILE KCSKGIYVVK
     LDTVDKLVIK YQKYWESMKI QLLRRQQLLQ QQQQQQQQGM DPNRAQNSQQ QQQQNQANMQ
     QARNRKPTKN QTTPAIAASV AMNMNDKGAS MSPALQKAGS AVPNFAQQMS PNMTPGTIPP
     TNVLSPHSQS HIPMVSPTMA KAASAAALKN DTASSSRRGS TKPRGKSTAP VTGKKTSNAP
     TPQVVPATVP STTNLSAAGT PNIRNKSATP LTAGLSPKST IRSNSNTALA SAKTPSPMTV
     SIPQPGNSSV FKKEEEYLSK LQLRKEEIRF RQKQRLDILS SSPVDLFLTT VADCLGINDE
     EIELINKIPE TTADNINNTG KKKLTKAAQK LRDKEILNVS IQVGEKDKLI MSSKAPDKVM
     DYSISAMSLA AVFKNLSSTG SLNNIALSGS NATTSKDIGN IYSHTGGVKR KFDEVEISPN
     SNGSPSASIM SESKKIKIDS PEDMFVTHSS EAAKGTNNSS LMDSGKEGSC KSMAGSATEV
     NDTSIWDWNF WTSIE
 
 
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