MED20_MOUSE
ID MED20_MOUSE Reviewed; 212 AA.
AC Q9R0X0; Q3UJQ7; Q3V418; Q6PAR6;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 20;
DE AltName: Full=Mediator complex subunit 20;
DE AltName: Full=TRF-proximal protein homolog;
GN Name=Med20; Synonyms=Trfp;
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 [MRNA] (ISOFORM 1).
RA Crowley T.E.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Cerebellum;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP INTERACTION WITH PPARG.
RX PubMed=12037571; DOI=10.1038/417563a;
RA Ge K., Guermah M., Yuan C.-X., Ito M., Wallberg A.E., Spiegelman B.M.,
RA Roeder R.G.;
RT "Transcription coactivator TRAP220 is required for PPAR gamma 2-stimulated
RT adipogenesis.";
RL Nature 417:563-567(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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). {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 (By similarity). Interacts
CC with PPARG. {ECO:0000250, ECO:0000269|PubMed:12037571}.
CC -!- INTERACTION:
CC Q9R0X0; Q9CQI9: Med30; NbExp=2; IntAct=EBI-398698, EBI-309220;
CC Q9R0X0; Q9D7W5: Med8; NbExp=2; IntAct=EBI-398698, EBI-7990252;
CC Q9R0X0; Q9BUE0: MED18; Xeno; NbExp=6; IntAct=EBI-398698, EBI-394640;
CC Q9R0X0; Q6P2C8: MED27; Xeno; NbExp=2; IntAct=EBI-398698, EBI-394603;
CC Q9R0X0; Q9NX70: MED29; Xeno; NbExp=2; IntAct=EBI-398698, EBI-394656;
CC Q9R0X0; O75586: MED6; Xeno; NbExp=2; IntAct=EBI-398698, EBI-394624;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9R0X0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9R0X0-2; Sequence=VSP_028989, VSP_028990;
CC Name=3;
CC IsoId=Q9R0X0-3; Sequence=VSP_028987, VSP_028988;
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 20 family.
CC {ECO:0000305}.
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DR EMBL; AJ245617; CAB53514.1; -; mRNA.
DR EMBL; AK019130; BAE43254.1; -; mRNA.
DR EMBL; AK043396; BAC31536.1; -; mRNA.
DR EMBL; AK146345; BAE27098.1; -; mRNA.
DR EMBL; BC060122; AAH60122.1; -; mRNA.
DR CCDS; CCDS28851.1; -. [Q9R0X0-1]
DR RefSeq; NP_064432.1; NM_020048.3. [Q9R0X0-1]
DR PDB; 6W1S; EM; 4.02 A; O=3-200.
DR PDBsum; 6W1S; -.
DR AlphaFoldDB; Q9R0X0; -.
DR SMR; Q9R0X0; -.
DR BioGRID; 208167; 3.
DR ComplexPortal; CPX-3264; Core mediator complex.
DR CORUM; Q9R0X0; -.
DR IntAct; Q9R0X0; 13.
DR MINT; Q9R0X0; -.
DR STRING; 10090.ENSMUSP00000024778; -.
DR iPTMnet; Q9R0X0; -.
DR PhosphoSitePlus; Q9R0X0; -.
DR EPD; Q9R0X0; -.
DR MaxQB; Q9R0X0; -.
DR PaxDb; Q9R0X0; -.
DR PeptideAtlas; Q9R0X0; -.
DR PRIDE; Q9R0X0; -.
DR ProteomicsDB; 292188; -. [Q9R0X0-1]
DR ProteomicsDB; 292189; -. [Q9R0X0-2]
DR ProteomicsDB; 292190; -. [Q9R0X0-3]
DR DNASU; 56771; -.
DR Ensembl; ENSMUST00000024778; ENSMUSP00000024778; ENSMUSG00000092558. [Q9R0X0-1]
DR GeneID; 56771; -.
DR KEGG; mmu:56771; -.
DR UCSC; uc008cvr.1; mouse. [Q9R0X0-2]
DR UCSC; uc008cvs.1; mouse. [Q9R0X0-1]
DR CTD; 9477; -.
DR MGI; MGI:1929648; Med20.
DR VEuPathDB; HostDB:ENSMUSG00000092558; -.
DR eggNOG; KOG4309; Eukaryota.
DR GeneTree; ENSGT00390000002060; -.
DR HOGENOM; CLU_080044_1_0_1; -.
DR InParanoid; Q9R0X0; -.
DR OMA; QSTFSIC; -.
DR OrthoDB; 1112080at2759; -.
DR PhylomeDB; Q9R0X0; -.
DR TreeFam; TF315156; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 56771; 26 hits in 71 CRISPR screens.
DR ChiTaRS; Med20; mouse.
DR PRO; PR:Q9R0X0; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9R0X0; protein.
DR Bgee; ENSMUSG00000092558; Expressed in paneth cell and 263 other tissues.
DR Genevisible; Q9R0X0; MM.
DR GO; GO:0070847; C:core mediator complex; ISO:MGI.
DR GO; GO:0016592; C:mediator complex; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO: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:0016567; P:protein ubiquitination; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR InterPro; IPR013921; Mediator_Med20.
DR PANTHER; PTHR12465; PTHR12465; 1.
DR Pfam; PF08612; Med20; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..212
FT /note="Mediator of RNA polymerase II transcription subunit
FT 20"
FT /id="PRO_0000065732"
FT VAR_SEQ 58..68
FT /note="QAGKLMYVMHN -> NREEETQPVIM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028987"
FT VAR_SEQ 69..212
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028988"
FT VAR_SEQ 143..145
FT /note="EYG -> RPW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028989"
FT VAR_SEQ 146..212
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028990"
SQ SEQUENCE 212 AA; 23192 MW; 88E116D0A9764438 CRC64;
MGVTCVSQMP VAEGKSLQQT VELLTKKLEM LGAEKQGTFC VDCETYHTAA STLGSQGQAG
KLMYVMHNSE YPLSCFALFE NGPCLIADTN FDVLMVKLKG FFQSAKASKI ETRGTRYQYC
DFLVKVGTVT MGPSARGISV EVEYGPCVVA SDCWSLLLEF LQSFLGSHAP GAPTVFGNRH
DAVYGPADTM IQYMELFNKI RKQQQVPVAG IR
