MED6_HUMAN
ID MED6_HUMAN Reviewed; 246 AA.
AC O75586; B4DU17; B4E2P0; O15401; Q53FE3; Q53HJ3; Q6FHQ4; Q9BTH1; Q9UHL1;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 6;
DE AltName: Full=Activator-recruited cofactor 33 kDa component;
DE Short=ARC33;
DE AltName: Full=Mediator complex subunit 6;
DE Short=hMed6;
DE AltName: Full=Renal carcinoma antigen NY-REN-28;
GN Name=MED6; Synonyms=ARC33;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS
RP SPECTROMETRY, AND IDENTIFICATION IN A FORM OF THE MEDIATOR COMPLEX.
RX PubMed=9734358; DOI=10.1016/s1097-2765(00)80131-8;
RA Sun X., Zhang Y., Cho H., Rickert P., Lees E., Lane W.S., Reinberg D.;
RT "NAT, a human complex containing Srb polypeptides that functions as a
RT negative regulator of activated transcription.";
RL Mol. Cell 2:213-222(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Placenta, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Coronary arterial endothelium, and Testis;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-157 (ISOFORM 1).
RA Kim Y.-J.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-246 (ISOFORM 1), AND IDENTIFICATION AS A
RP RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [10]
RP PROTEIN SEQUENCE OF 200-208 AND 227-236, AND IDENTIFICATION IN THE ARC
RP COMPLEX.
RX PubMed=10235267; DOI=10.1038/19789;
RA Naeaer A.M., Beaurang P.A., Zhou S., Abraham S., Solomon W.B., Tjian R.;
RT "Composite co-activator ARC mediates chromatin-directed transcriptional
RT activation.";
RL Nature 398:828-832(1999).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SMCC
RP COMPLEX.
RX PubMed=10024883; DOI=10.1016/s1097-2765(00)80178-1;
RA Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E.,
RA Qin J., Roeder R.G.;
RT "A novel human SRB/MED-containing cofactor complex, SMCC, involved in
RT transcription regulation.";
RL Mol. Cell 3:97-108(1999).
RN [12]
RP ERRATUM OF PUBMED:10024883.
RA Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E.,
RA Qin J., Roeder R.G.;
RL Mol. Cell 3:541-541(1999).
RN [13]
RP INTERACTION WITH CCNC; MED10 AND MED23.
RX PubMed=10993082; DOI=10.1038/35024111;
RA Akoulitchev S., Chuikov S., Reinberg D.;
RT "TFIIH is negatively regulated by cdk8-containing mediator complexes.";
RL Nature 407:102-106(2000).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR
RP COMPLEX, AND INTERACTION OF THE MEDIATOR COMPLEX WITH ESR1 AND ESR2.
RX PubMed=11867769; DOI=10.1073/pnas.261715899;
RA Kang Y.K., Guermah M., Yuan C.-X., Roeder R.G.;
RT "The TRAP/Mediator coactivator complex interacts directly with estrogen
RT receptors alpha and beta through the TRAP220 subunit and directly enhances
RT estrogen receptor function in vitro.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2642-2647(2002).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MEDIATOR
RP COMPLEX.
RX PubMed=15175163; DOI=10.1016/j.molcel.2004.05.006;
RA Sato S., Tomomori-Sato C., Parmely T.J., Florens L., Zybailov B.,
RA Swanson S.K., Banks C.A.S., Jin J., Cai Y., Washburn M.P., Conaway J.W.,
RA Conaway R.C.;
RT "A set of consensus mammalian mediator subunits identified by
RT multidimensional protein identification technology.";
RL Mol. Cell 14:685-691(2004).
RN [16]
RP INTERACTION WITH MED1; MED21 AND MED30, IDENTIFICATION BY MASS
RP SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, AND ASSOCIATION OF
RP THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
RX PubMed=15989967; DOI=10.1016/j.molcel.2005.05.015;
RA Zhang X., Krutchinsky A., Fukuda A., Chen W., Yamamura S., Chait B.T.,
RA Roeder R.G.;
RT "MED1/TRAP220 exists predominantly in a TRAP/Mediator subpopulation
RT enriched in RNA polymerase II and is required for ER-mediated
RT transcription.";
RL Mol. Cell 19:89-100(2005).
RN [17]
RP ASSOCIATION WITH PROMOTER REGIONS.
RX PubMed=16574658; DOI=10.1074/jbc.m600163200;
RA Udayakumar T.S., Belakavadi M., Choi K.-H., Pandey P.K., Fondell J.D.;
RT "Regulation of Aurora-A kinase gene expression via GABP recruitment of
RT TRAP220/MED1.";
RL J. Biol. Chem. 281:14691-14699(2006).
RN [18]
RP FUNCTION, AND INTERACTION WITH MED 1 AND MED10.
RX PubMed=16595664; DOI=10.1074/jbc.m601983200;
RA Baek H.J., Kang Y.K., Roeder R.G.;
RT "Human Mediator enhances basal transcription by facilitating recruitment of
RT transcription factor IIB during preinitiation complex assembly.";
RL J. Biol. Chem. 281:15172-15181(2006).
RN [19]
RP INTERACTION WITH CDK8; CTNNB1 AND GLI3.
RX PubMed=17000779; DOI=10.1128/mcb.00443-06;
RA Zhou H., Kim S., Ishii S., Boyer T.G.;
RT "Mediator modulates Gli3-dependent Sonic hedgehog signaling.";
RL Mol. Cell. Biol. 26:8667-8682(2006).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-236 AND LYS-241, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-208, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
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. {ECO:0000269|PubMed:16595664}.
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 CTNNB1 and
CC GLI3. {ECO:0000269|PubMed:10024883, ECO:0000269|PubMed:10235267,
CC ECO:0000269|PubMed:10993082, ECO:0000269|PubMed:11867769,
CC ECO:0000269|PubMed:15175163, ECO:0000269|PubMed:15989967,
CC ECO:0000269|PubMed:16595664, ECO:0000269|PubMed:17000779,
CC ECO:0000269|PubMed:9734358}.
CC -!- INTERACTION:
CC O75586; Q13616: CUL1; NbExp=2; IntAct=EBI-394624, EBI-359390;
CC O75586; Q9NVC6: MED17; NbExp=2; IntAct=EBI-394624, EBI-394562;
CC O75586; Q9BUE0: MED18; NbExp=3; IntAct=EBI-394624, EBI-394640;
CC O75586; Q6P2C8: MED27; NbExp=2; IntAct=EBI-394624, EBI-394603;
CC O75586; Q9NX70: MED29; NbExp=3; IntAct=EBI-394624, EBI-394656;
CC O75586; Q9R0X0: Med20; Xeno; NbExp=2; IntAct=EBI-394624, EBI-398698;
CC O75586; Q9D7W5: Med8; Xeno; NbExp=2; IntAct=EBI-394624, EBI-7990252;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O75586-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75586-2; Sequence=VSP_054589;
CC Name=3;
CC IsoId=O75586-3; Sequence=VSP_054590;
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 6 family.
CC {ECO:0000305}.
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DR EMBL; AF074723; AAC26869.1; -; mRNA.
DR EMBL; BT006831; AAP35477.1; -; mRNA.
DR EMBL; CR541697; CAG46498.1; -; mRNA.
DR EMBL; AK300460; BAG62179.1; -; mRNA.
DR EMBL; AK304361; BAG65202.1; -; mRNA.
DR EMBL; AK222587; BAD96307.1; -; mRNA.
DR EMBL; AK223346; BAD97066.1; -; mRNA.
DR EMBL; AL357153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004106; AAH04106.1; -; mRNA.
DR EMBL; U78082; AAB84363.1; -; mRNA.
DR EMBL; AF155104; AAD42870.1; -; mRNA.
DR CCDS; CCDS61483.1; -. [O75586-3]
DR CCDS; CCDS61484.1; -. [O75586-2]
DR CCDS; CCDS9805.1; -. [O75586-1]
DR RefSeq; NP_001271138.1; NM_001284209.1. [O75586-2]
DR RefSeq; NP_001271139.1; NM_001284210.1. [O75586-3]
DR RefSeq; NP_001271140.1; NM_001284211.1.
DR RefSeq; NP_005457.2; NM_005466.3. [O75586-1]
DR PDB; 7EMF; EM; 3.50 A; F=1-246.
DR PDB; 7ENA; EM; 4.07 A; f=1-246.
DR PDB; 7ENC; EM; 4.13 A; f=1-246.
DR PDB; 7ENJ; EM; 4.40 A; F=1-246.
DR PDB; 7LBM; EM; 4.80 A; g=1-246.
DR PDB; 7NVR; EM; 4.50 A; a=1-246.
DR PDBsum; 7EMF; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7ENJ; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR AlphaFoldDB; O75586; -.
DR SMR; O75586; -.
DR BioGRID; 115319; 92.
DR ComplexPortal; CPX-3227; Core mediator complex.
DR CORUM; O75586; -.
DR DIP; DIP-31456N; -.
DR IntAct; O75586; 47.
DR MINT; O75586; -.
DR STRING; 9606.ENSP00000481920; -.
DR iPTMnet; O75586; -.
DR PhosphoSitePlus; O75586; -.
DR BioMuta; MED6; -.
DR EPD; O75586; -.
DR jPOST; O75586; -.
DR MassIVE; O75586; -.
DR MaxQB; O75586; -.
DR PaxDb; O75586; -.
DR PeptideAtlas; O75586; -.
DR PRIDE; O75586; -.
DR ProteomicsDB; 50100; -. [O75586-1]
DR ProteomicsDB; 5142; -.
DR ProteomicsDB; 5839; -.
DR Antibodypedia; 25135; 297 antibodies from 28 providers.
DR DNASU; 10001; -.
DR Ensembl; ENST00000256379.10; ENSP00000256379.5; ENSG00000133997.12. [O75586-1]
DR Ensembl; ENST00000430055.6; ENSP00000413343.2; ENSG00000133997.12. [O75586-2]
DR Ensembl; ENST00000440435.2; ENSP00000394502.2; ENSG00000133997.12. [O75586-3]
DR GeneID; 10001; -.
DR KEGG; hsa:10001; -.
DR MANE-Select; ENST00000256379.10; ENSP00000256379.5; NM_005466.4; NP_005457.2.
DR UCSC; uc001xmf.5; human. [O75586-1]
DR CTD; 10001; -.
DR GeneCards; MED6; -.
DR HGNC; HGNC:19970; MED6.
DR HPA; ENSG00000133997; Low tissue specificity.
DR MIM; 602984; gene.
DR neXtProt; NX_O75586; -.
DR OpenTargets; ENSG00000133997; -.
DR PharmGKB; PA134868263; -.
DR VEuPathDB; HostDB:ENSG00000133997; -.
DR eggNOG; KOG3169; Eukaryota.
DR GeneTree; ENSGT00390000017666; -.
DR HOGENOM; CLU_077754_1_0_1; -.
DR InParanoid; O75586; -.
DR OMA; HLHNMIG; -.
DR OrthoDB; 1251252at2759; -.
DR PhylomeDB; O75586; -.
DR TreeFam; TF313577; -.
DR PathwayCommons; O75586; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR SignaLink; O75586; -.
DR SIGNOR; O75586; -.
DR BioGRID-ORCS; 10001; 765 hits in 1095 CRISPR screens.
DR GeneWiki; MED6; -.
DR GenomeRNAi; 10001; -.
DR Pharos; O75586; Tbio.
DR PRO; PR:O75586; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; O75586; protein.
DR Bgee; ENSG00000133997; Expressed in calcaneal tendon and 178 other tissues.
DR ExpressionAtlas; O75586; baseline and differential.
DR Genevisible; O75586; HS.
DR GO; GO:0070847; C:core mediator complex; IPI:ComplexPortal.
DR GO; GO:0016592; C:mediator complex; IDA:MGI.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA: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: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:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR Gene3D; 3.10.450.580; -; 1.
DR InterPro; IPR007018; Mediator_Med6.
DR InterPro; IPR016820; Mediator_Med6_met/pln.
DR InterPro; IPR038566; Mediator_Med6_sf.
DR PANTHER; PTHR13104; PTHR13104; 1.
DR Pfam; PF04934; Med6; 1.
DR PIRSF; PIRSF023869; Mediator_MED6_meta/pln; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Direct protein sequencing; Isopeptide bond; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..246
FT /note="Mediator of RNA polymerase II transcription subunit
FT 6"
FT /id="PRO_0000096388"
FT REGION 193..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 236
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 241
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 208
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 119
FT /note="V -> VSLFSFYK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054589"
FT VAR_SEQ 156..246
FT /note="DKVRPKAKRKEEPSSIFQRQRVDALLLDLRQKFPPKFVQLKPGEKPVPVDQT
FT KKEAEPIPETVKPEEKETTKNVQQTVSAKGPPEKRMRLQ -> AKAWRKACSSGSNKER
FT GRTYTRNCKT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054590"
FT CONFLICT 151
FT /note="D -> V (in Ref. 1; AAC26869)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="D -> G (in Ref. 9; AAB84363)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="P -> S (in Ref. 5; BAD97066)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="E -> G (in Ref. 5; BAD96307)"
FT /evidence="ECO:0000305"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 56..61
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 91..101
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 111..136
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 174..187
FT /evidence="ECO:0007829|PDB:7EMF"
SQ SEQUENCE 246 AA; 28425 MW; 9B173626F583B48B CRC64;
MAAVDIRDNL LGISWVDSSW IPILNSGSVL DYFSERSNPF YDRTCNNEVV KMQRLTLEHL
NQMVGIEYIL LHAQEPILFI IRKQQRQSPA QVIPLADYYI IAGVIYQAPD LGSVINSRVL
TAVHGIQSAF DEAMSYCRYH PSKGYWWHFK DHEEQDKVRP KAKRKEEPSS IFQRQRVDAL
LLDLRQKFPP KFVQLKPGEK PVPVDQTKKE AEPIPETVKP EEKETTKNVQ QTVSAKGPPE
KRMRLQ
