MED25_MOUSE
ID MED25_MOUSE Reviewed; 745 AA.
AC Q8VCB2; Q3UDX6; Q3UFQ1; Q6IR27;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 25;
DE AltName: Full=Mediator complex subunit 25;
DE Short=mMED25;
GN Name=Med25;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-522 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Kidney, Mammary tumor, and Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH RARA AND RXRA.
RX PubMed=17641689; DOI=10.1038/sj.emboj.7601797;
RA Lee H.-K., Park U.-H., Kim E.-J., Um S.-J.;
RT "MED25 is distinct from TRAP220/MED1 in cooperating with CBP for retinoid
RT receptor activation.";
RL EMBO J. 26:3545-3557(2007).
RN [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-723, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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 and THRB in a ligand-dependent fashion. Binds
CC the Herpes simplex virus activator VP16 (By similarity). Interacts with
CC RARA and RXRA in a ligand-dependent fashion. {ECO:0000250,
CC ECO:0000269|PubMed:17641689}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8VCB2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VCB2-2; Sequence=VSP_028147, VSP_028150;
CC Name=3;
CC IsoId=Q8VCB2-3; Sequence=VSP_028148;
CC Name=4;
CC IsoId=Q8VCB2-4; Sequence=VSP_028149;
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 25 family.
CC {ECO:0000305}.
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DR EMBL; AK148368; BAE28509.1; -; mRNA.
DR EMBL; AK149867; BAE29135.1; -; mRNA.
DR EMBL; BC021333; AAH21333.1; -; mRNA.
DR EMBL; BC031138; AAH31138.1; -; mRNA.
DR EMBL; BC071206; AAH71206.1; -; mRNA.
DR CCDS; CCDS21220.1; -. [Q8VCB2-1]
DR CCDS; CCDS85291.1; -. [Q8VCB2-2]
DR RefSeq; NP_001318135.1; NM_001331206.1.
DR RefSeq; NP_001318137.1; NM_001331208.1. [Q8VCB2-2]
DR RefSeq; NP_083641.1; NM_029365.3. [Q8VCB2-1]
DR PDB; 6W1S; EM; 4.02 A; T=15-216.
DR PDBsum; 6W1S; -.
DR AlphaFoldDB; Q8VCB2; -.
DR BMRB; Q8VCB2; -.
DR SMR; Q8VCB2; -.
DR BioGRID; 217616; 2.
DR ComplexPortal; CPX-3264; Core mediator complex.
DR IntAct; Q8VCB2; 5.
DR MINT; Q8VCB2; -.
DR STRING; 10090.ENSMUSP00000003049; -.
DR iPTMnet; Q8VCB2; -.
DR PhosphoSitePlus; Q8VCB2; -.
DR EPD; Q8VCB2; -.
DR MaxQB; Q8VCB2; -.
DR PaxDb; Q8VCB2; -.
DR PeptideAtlas; Q8VCB2; -.
DR PRIDE; Q8VCB2; -.
DR ProteomicsDB; 295867; -. [Q8VCB2-1]
DR ProteomicsDB; 295868; -. [Q8VCB2-2]
DR ProteomicsDB; 295869; -. [Q8VCB2-3]
DR ProteomicsDB; 295870; -. [Q8VCB2-4]
DR Antibodypedia; 45928; 123 antibodies from 20 providers.
DR Ensembl; ENSMUST00000003049; ENSMUSP00000003049; ENSMUSG00000002968. [Q8VCB2-1]
DR Ensembl; ENSMUST00000207278; ENSMUSP00000146595; ENSMUSG00000002968. [Q8VCB2-2]
DR GeneID; 75613; -.
DR KEGG; mmu:75613; -.
DR UCSC; uc009grm.1; mouse. [Q8VCB2-2]
DR UCSC; uc009grn.1; mouse. [Q8VCB2-1]
DR UCSC; uc009grs.1; mouse. [Q8VCB2-3]
DR CTD; 81857; -.
DR MGI; MGI:1922863; Med25.
DR VEuPathDB; HostDB:ENSMUSG00000002968; -.
DR eggNOG; ENOG502QRN5; Eukaryota.
DR GeneTree; ENSGT00940000160439; -.
DR HOGENOM; CLU_007594_0_0_1; -.
DR InParanoid; Q8VCB2; -.
DR OrthoDB; 340324at2759; -.
DR PhylomeDB; Q8VCB2; -.
DR TreeFam; TF329598; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 75613; 14 hits in 73 CRISPR screens.
DR ChiTaRS; Med25; mouse.
DR PRO; PR:Q8VCB2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8VCB2; protein.
DR Bgee; ENSMUSG00000002968; Expressed in dorsal pancreas and 255 other tissues.
DR ExpressionAtlas; Q8VCB2; baseline and differential.
DR Genevisible; Q8VCB2; MM.
DR GO; GO:0070847; C:core mediator complex; ISO:MGI.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IPI:MGI.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; IPI:UniProtKB.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IPI:UniProtKB.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0035563; P:positive regulation of chromatin binding; ISO:MGI.
DR GO; GO:2001178; P:positive regulation of mediator complex assembly; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Methylation; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..745
FT /note="Mediator of RNA polymerase II transcription subunit
FT 25"
FT /id="PRO_0000304953"
FT REGION 1..226
FT /note="Interaction with the Mediator complex"
FT /evidence="ECO:0000250"
FT REGION 233..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..374
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 563..652
FT /note="Interaction with RARA"
FT /evidence="ECO:0000250"
FT REGION 584..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..705
FT /note="Interaction with RARA"
FT /evidence="ECO:0000250"
FT MOTIF 645..649
FT /note="LXXLL motif"
FT COMPBIAS 319..345
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..636
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..678
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 723
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 1..103
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028147"
FT VAR_SEQ 102
FT /note="K -> KPVLGAEPYPDPARMSNSLSLLPANGIPRKLSSGIVKCRCLLRTSGR
FT NPHLEFWEAPRPSLLHIRDGAYEDSTTFGQM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028148"
FT VAR_SEQ 103..745
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028149"
FT VAR_SEQ 558..581
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028150"
SQ SEQUENCE 745 AA; 78113 MW; A8C63CF063BECEEA CRC64;
MVPGSEGPAR AGGLVADVVF VIEGTANLGP YFEELRKHYL LPAIEYFNGG PPAETDFGGD
YGGTQYSLVV FNTVDCAPES YVQCHAPTSS AYEFVTWLDG IKFMGGGGES CSLIAEGLST
ALQLFDDFKK MREQIGQTHR VCLLICNSPP YLLPAVESTT YSGCTTESLV QKIGERGIHF
SIVSPRKLPA LRLLFEKAAP PALLEPLQQP ADVSQDPRHM VLVRGLVLPV GGSSTSGSLQ
TKQAVPLPPA PASAATLSAA PPQALPPVPP QYQVPGNLSA AQVAAQNAVE AAKSQKAGLG
PRFSPINPLQ QAAPGVGPPF SQAPAPPLAP VPPGAPKPPP ASQPSLVSTV APGPVLAAPA
QPGAPSLAGT VTPGGVNGPS AAQLGGPALG GQQSVSNKLL AWSGVLEWQE KPKPASVDAN
TKLTRSLPCQ VYVNHGENLK TEQWPQKLIM QLIPQQLLTT LGPLFRNSRM VQFHFTNKDL
ESLKGLYRIM GNGFAGCVHF PHTAPCEVRV LMLLYSSKKK IFMGLIPYDQ SGFVNGIRQV
ITNHKQVQQQ KLEQQRGMGA QQAPPVLGPI LEEQARPPQN LLQLRAPQPQ PQGAVGASAA
TGQPQPQGAT QAPTGAPQGP PGAAPGPPPS GPILRPQNPG ANPQLRSLLL NPAPPQTGVP
PPQASLHHLQ PPGAPTLLPP HQSMGQPQLG PQLLHPPPAQ SWPTQLPQRA PLPGQMLLSG
GPRGPVPQPG LQPSVMEDDI LMDLI
