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MED25_BOVIN
ID   MED25_BOVIN             Reviewed;         746 AA.
AC   A2VE44;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 25;
DE   AltName: Full=Mediator complex subunit 25;
GN   Name=MED25;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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. Required for RARA/RXRA-mediated
CC       transcription (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the Mediator complex, which is composed of MED1,
CC       MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L,
CC       MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23,
CC       MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and
CC       CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct
CC       module termed the CDK8 module. Mediator containing the CDK8 module is
CC       less active than Mediator lacking this module in supporting
CC       transcriptional activation. Individual preparations of the Mediator
CC       complex lacking one or more distinct subunits have been variously
CC       termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. Interacts with CREBBP.
CC       Interacts with ESR1, GR, RARA, RXRA and THRB in a ligand-dependent
CC       fashion. Binds the Herpes simplex virus activator VP16 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 25 family.
CC       {ECO:0000305}.
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DR   EMBL; BC133565; AAI33566.1; -; mRNA.
DR   RefSeq; NP_001075914.1; NM_001082445.1.
DR   AlphaFoldDB; A2VE44; -.
DR   BMRB; A2VE44; -.
DR   SMR; A2VE44; -.
DR   STRING; 9913.ENSBTAP00000040773; -.
DR   PRIDE; A2VE44; -.
DR   Ensembl; ENSBTAT00000043183; ENSBTAP00000040773; ENSBTAG00000008518.
DR   GeneID; 533865; -.
DR   KEGG; bta:533865; -.
DR   CTD; 81857; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008518; -.
DR   VGNC; VGNC:31362; MED25.
DR   eggNOG; ENOG502QRN5; Eukaryota.
DR   GeneTree; ENSGT00940000160439; -.
DR   InParanoid; A2VE44; -.
DR   OMA; NDQQKIP; -.
DR   OrthoDB; 340324at2759; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000008518; Expressed in laryngeal cartilage and 104 other tissues.
DR   ExpressionAtlas; A2VE44; baseline.
DR   GO; GO:0070847; C:core mediator complex; IEA:Ensembl.
DR   GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0046965; F:nuclear retinoid X receptor binding; IEA:Ensembl.
DR   GO; GO:0001223; F:transcription coactivator binding; IEA:Ensembl.
DR   GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0035563; P:positive regulation of chromatin binding; IEA:Ensembl.
DR   GO; GO:2001178; P:positive regulation of mediator complex assembly; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 2.40.290.30; -; 1.
DR   InterPro; IPR045105; Med25/PTOV1.
DR   InterPro; IPR021394; Med25_PTOV.
DR   InterPro; IPR038196; Med25_PTOV_sf.
DR   InterPro; IPR021406; Mediator_Med25_NR-box.
DR   InterPro; IPR021397; Mediator_Med25_SD1.
DR   InterPro; IPR021419; Mediator_Med25_VWA.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR12433; PTHR12433; 1.
DR   Pfam; PF11232; Med25; 1.
DR   Pfam; PF11244; Med25_NR-box; 1.
DR   Pfam; PF11235; Med25_SD1; 1.
DR   Pfam; PF11265; Med25_VWA; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
PE   2: Evidence at transcript level;
KW   Activator; Methylation; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..746
FT                   /note="Mediator of RNA polymerase II transcription subunit
FT                   25"
FT                   /id="PRO_0000304951"
FT   REGION          1..226
FT                   /note="Interaction with the Mediator complex"
FT                   /evidence="ECO:0000250"
FT   REGION          233..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..543
FT                   /note="Interaction with VP16"
FT                   /evidence="ECO:0000250"
FT   REGION          395..545
FT                   /note="Interaction with CREBBP"
FT                   /evidence="ECO:0000250"
FT   REGION          548..746
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..652
FT                   /note="Interaction with RARA"
FT                   /evidence="ECO:0000250"
FT   REGION          639..706
FT                   /note="Interaction with RARA"
FT                   /evidence="ECO:0000250"
FT   MOTIF           645..649
FT                   /note="LXXLL motif"
FT   COMPBIAS        306..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..345
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..637
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        648..705
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         724
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VCB2"
SQ   SEQUENCE   746 AA;  78110 MW;  F2F43D6AE943496A CRC64;
     MVPGSEGPAR AGGLVADVVF VIEGTANLGP YFEGLRKHYL LPAIEYFNGG PPAETDFGGD
     YGGTQYSLVV FNTVDCAPES YVQCHAPTSS AYEFVTWLDG IKFMGGGGES CSLIAEGLST
     ALQLFDDFKK MREQIGQTHR VCLLICNSPP YLLPAVESTT YSGCTTETLV QKIGERGIYF
     SIVSPRKLPA LRLLFEKAAP PAMLEPLQPP ADVSQDPRHM VLVRGLVLPV GGGSAPGPLQ
     PKQPVPLPPA APAGATLSTA PQQPLPPVPQ QYQVPGNLSA AQVAAQNAVE AAKNQKAGLG
     PRFSPINPLQ QATPGVGPPY SQTQATQLPP GPPGAPKPPP ASQPSLVSTV APGPGLAPPA
     QPGAPSMAGT VAPGGVSGPS PAQLGAPALG GQQSVSNKLL AWSGVLEWQE KPKPASVDAN
     TKLTRSLPCQ VYVNHGENLK TEQWPQKLIM QLIPQQLLTT LGPLFRNSRM VQFHFTNKDL
     DSLKGLYRIM GNGFAGCVHF PHTAPCEVRV LMLLYSSKKK IFMGLIPYDQ SGFVNGIRQV
     ITNHKQVQQQ KLEQQRGMGA QQAPPGLGPI LEDQARPSQN LLQLRPPQPQ PQGTVGASAA
     AGQPQPQGAA PAPPGAPQGP PGAAPGPPPP GPLLRPQNPG ANPQLRSLLL NPPPPQTGVP
     PPQASLHHLQ PPGAPALLPP PHQGLGQPQL GPPLLHPPPA QSWPAQLPPR ASLPGQMLLS
     GGPRGPVPQP GLQPSVMEDD ILMDLI
 
 
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