MED8_MOUSE
ID MED8_MOUSE Reviewed; 268 AA.
AC Q9D7W5; Q3UGB4; Q99LM4; Q9JJ84;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 8;
DE AltName: Full=Activator-recruited cofactor 32 kDa component;
DE Short=ARC32;
DE AltName: Full=Mediator complex subunit 8;
GN Name=Med8; ORFNames=MNCb-2386;
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].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, and Stomach;
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].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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. May play a role as a target
CC recruitment subunit in E3 ubiquitin-protein ligase complexes and thus
CC in ubiquitination and subsequent proteasomal degradation of target
CC proteins (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
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. May be part of a
CC multisubunit E3 ubiquitin-protein ligase complex with the Elongin BC
CC complex (ELOB and ELOC), CUL2 and RBX1 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9D7W5; Q9R0X0: Med20; NbExp=2; IntAct=EBI-7990252, EBI-398698;
CC Q9D7W5; Q9CQI9: Med30; NbExp=2; IntAct=EBI-7990252, EBI-309220;
CC Q9D7W5; Q9NVC6: MED17; Xeno; NbExp=2; IntAct=EBI-7990252, EBI-394562;
CC Q9D7W5; Q15528: MED22; Xeno; NbExp=2; IntAct=EBI-7990252, EBI-394687;
CC Q9D7W5; Q6P2C8: MED27; Xeno; NbExp=2; IntAct=EBI-7990252, EBI-394603;
CC Q9D7W5; Q9H204: MED28; Xeno; NbExp=2; IntAct=EBI-7990252, EBI-514199;
CC Q9D7W5; Q9NX70: MED29; Xeno; NbExp=2; IntAct=EBI-7990252, EBI-394656;
CC Q9D7W5; O75586: MED6; Xeno; NbExp=2; IntAct=EBI-7990252, EBI-394624;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 8 family.
CC {ECO:0000305}.
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DR EMBL; AB041805; BAA95113.1; -; mRNA.
DR EMBL; AK008759; BAB25879.1; -; mRNA.
DR EMBL; AK147032; BAE27624.1; -; mRNA.
DR EMBL; AK148025; BAE28295.1; -; mRNA.
DR EMBL; BC002315; AAH02315.1; -; mRNA.
DR EMBL; BC021870; AAH21870.1; -; mRNA.
DR CCDS; CCDS38854.1; -.
DR RefSeq; NP_001277617.1; NM_001290688.1.
DR RefSeq; NP_064384.2; NM_020000.3.
DR RefSeq; NP_776067.1; NM_173719.3.
DR PDB; 6W1S; EM; 4.02 A; E=7-186.
DR PDBsum; 6W1S; -.
DR AlphaFoldDB; Q9D7W5; -.
DR SMR; Q9D7W5; -.
DR BioGRID; 219788; 3.
DR ComplexPortal; CPX-3264; Core mediator complex.
DR IntAct; Q9D7W5; 12.
DR MINT; Q9D7W5; -.
DR STRING; 10090.ENSMUSP00000019229; -.
DR iPTMnet; Q9D7W5; -.
DR PhosphoSitePlus; Q9D7W5; -.
DR EPD; Q9D7W5; -.
DR jPOST; Q9D7W5; -.
DR MaxQB; Q9D7W5; -.
DR PaxDb; Q9D7W5; -.
DR PeptideAtlas; Q9D7W5; -.
DR PRIDE; Q9D7W5; -.
DR ProteomicsDB; 292289; -.
DR Antibodypedia; 32328; 180 antibodies from 28 providers.
DR DNASU; 80509; -.
DR Ensembl; ENSMUST00000019229; ENSMUSP00000019229; ENSMUSG00000006392.
DR GeneID; 80509; -.
DR KEGG; mmu:80509; -.
DR UCSC; uc008ujw.2; mouse.
DR CTD; 112950; -.
DR MGI; MGI:1915269; Med8.
DR VEuPathDB; HostDB:ENSMUSG00000006392; -.
DR eggNOG; KOG3583; Eukaryota.
DR GeneTree; ENSGT00390000011838; -.
DR InParanoid; Q9D7W5; -.
DR OMA; IIMRVND; -.
DR OrthoDB; 1392867at2759; -.
DR PhylomeDB; Q9D7W5; -.
DR TreeFam; TF316778; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 80509; 30 hits in 77 CRISPR screens.
DR PRO; PR:Q9D7W5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D7W5; protein.
DR Bgee; ENSMUSG00000006392; Expressed in ectoderm and 258 other tissues.
DR ExpressionAtlas; Q9D7W5; baseline and differential.
DR Genevisible; Q9D7W5; MM.
DR GO; GO:0070847; C:core mediator complex; ISO:MGI.
DR GO; GO:0016592; C:mediator complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
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; IEA:UniProtKB-UniPathway.
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 InterPro; IPR019364; Mediatior_Med8_fun/met.
DR PANTHER; PTHR13074; PTHR13074; 1.
DR Pfam; PF10232; Med8; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Coiled coil; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation pathway.
FT CHAIN 1..268
FT /note="Mediator of RNA polymerase II transcription subunit
FT 8"
FT /id="PRO_0000096395"
FT REGION 142..151
FT /note="Interaction with the Elongin BC complex"
FT /evidence="ECO:0000250"
FT REGION 156..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..29
FT /evidence="ECO:0000255"
FT COILED 133..163
FT /evidence="ECO:0000255"
FT COMPBIAS 224..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96G25"
FT CONFLICT 57
FT /note="N -> NSFALLSGQLN (in Ref. 1; BAA95113)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 268 AA; 29199 MW; 20A0C02E00BCA667 CRC64;
MQREEKQLEA SLDALLNQVA DLKNSLGSFI YKLENEYDRL TWPSVLDSFA LLSGQLNTLN
KVLKHEKTPL FRNQVIIPLV LSPDRDEDLM RQTEGRVPVF SHEVVPDHLR TKPDPEVEEQ
EKQLTTDAAR IGADAAQKQI QSLNKMCSNL LEKISKEERE SESGGLRPNK QTFNPGDTNA
LVAAVAFGKG LSNWRPSGSS GPGQPGQPGA GTILAGASGL PQVQMPGAPN QQQPMLSGVQ
MAQAGQPGKM PSGIKTNIKS ASMHPYQR
