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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
 
 
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