MED15_HUMAN
ID MED15_HUMAN Reviewed; 788 AA.
AC Q96RN5; D3DX31; D3DX32; O15413; Q6IC31; Q8NF16; Q96CT0; Q96IH7; Q9P1T3;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 15;
DE AltName: Full=Activator-recruited cofactor 105 kDa component;
DE Short=ARC105;
DE AltName: Full=CTG repeat protein 7a;
DE AltName: Full=Mediator complex subunit 15;
DE AltName: Full=Positive cofactor 2 glutamine/Q-rich-associated protein;
DE Short=PC2 glutamine/Q-rich-associated protein;
DE AltName: Full=TPA-inducible gene 1 protein;
DE Short=TIG-1;
DE AltName: Full=Trinucleotide repeat-containing gene 7 protein;
GN Name=MED15; Synonyms=ARC105, CTG7A, PCQAP, TIG1, TNRC7;
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 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC TISSUE=Megakaryocyte, and Placenta;
RX PubMed=11024300; DOI=10.1016/s0378-1119(00)00292-4;
RA Abraham S., Solomon W.B.;
RT "A novel glutamine-rich putative transcriptional adaptor protein (TIG-1),
RT preferentially expressed in placental and bone-marrow tissues.";
RL Gene 255:389-400(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND POLYMORPHISM OF POLY-GLN
RP REGION.
RC TISSUE=Cervix carcinoma;
RX PubMed=11414760; DOI=10.1006/geno.2001.6566;
RA Berti L., Mittler G., Przemeck G.K.H., Stelzer G., Guenzler B., Amati F.,
RA Conti E., Dallapiccola B., Hrabe' de Angelis M., Novelli G.,
RA Meisterernst M.;
RT "Isolation and characterization of a novel gene from the DiGeorge
RT chromosomal region that encodes for a mediator subunit.";
RL Genomics 74:320-332(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Hepatoma, and Spleen;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 405-788 (ISOFORM 1).
RC TISSUE=Eye, and Kidney;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 185-573 (ISOFORM 2).
RC TISSUE=Brain cortex;
RX PubMed=9225980; DOI=10.1007/s004390050476;
RA Margolis R.L., Abraham M.R., Gatchell S.B., Li S.-H., Kidwai A.S.,
RA Breschel T.S., Stine O.C., Callahan C., McInnis M.G., Ross C.A.;
RT "cDNAs with long CAG trinucleotide repeats from human brain.";
RL Hum. Genet. 100:114-122(1997).
RN [8]
RP IDENTIFICATION IN ARC COMPLEX, AND PROTEIN SEQUENCE OF 39-48 AND 525-536.
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 [9]
RP FUNCTION, AND INTERACTION WITH SMAD1; SMAD2 AND SMAD3.
RX PubMed=12167862; DOI=10.1038/nature00969;
RA Kato Y., Habas R., Katsuyama Y., Naeaer A.M., He X.;
RT "A component of the ARC/Mediator complex required for TGF beta/Nodal
RT signalling.";
RL Nature 418:641-646(2002).
RN [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR
RP COMPLEX, AND ASSOCIATION OF 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 [12]
RP INTERACTION WITH TRIM11, UBIQUITINATION, AND SUBCELLULAR LOCATION.
RX PubMed=16904669; DOI=10.1016/j.febslet.2006.07.066;
RA Ishikawa H., Tachikawa H., Miura Y., Takahashi N.;
RT "TRIM11 binds to and destabilizes a key component of the activator-mediated
RT cofactor complex (ARC105) through the ubiquitin-proteasome system.";
RL FEBS Lett. 580:4784-4792(2006).
RN [13]
RP FUNCTION.
RX PubMed=16630888; DOI=10.1016/j.molcel.2006.03.023;
RA Andrau J.-C., van de Pasch L., Lijnzaad P., Bijma T., Koerkamp M.G.,
RA van de Peppel J., Werner M., Holstege F.C.P.;
RT "Genome-wide location of the coactivator mediator: binding without
RT activation and transient Cdk8 interaction on DNA.";
RL Mol. Cell 22:179-192(2006).
RN [14]
RP INTERACTION WITH WWTR1.
RX PubMed=18568018; DOI=10.1038/ncb1748;
RA Varelas X., Sakuma R., Samavarchi-Tehrani P., Peerani R., Rao B.M.,
RA Dembowy J., Yaffe M.B., Zandstra P.W., Wrana J.L.;
RT "TAZ controls Smad nucleocytoplasmic shuttling and regulates human
RT embryonic stem-cell self-renewal.";
RL Nat. Cell Biol. 10:837-848(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-603, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-603, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-603, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP STRUCTURE BY NMR OF 5-78, FUNCTION, INTERACTION WITH SREBF1 AND SREBF2, AND
RP MUTAGENESIS OF GLU-42; LEU-58 AND ALA-60.
RX PubMed=16799563; DOI=10.1038/nature04942;
RA Yang F., Vought B.W., Satterlee J.S., Walker A.K., Jim Sun Z.-Y.,
RA Watts J.L., DeBeaumont R., Saito R.M., Hyberts S.G., Yang S., Macol C.,
RA Iyer L., Tjian R., van den Heuvel S., Hart A.C., Wagner G., Naeaer A.M.;
RT "An ARC/Mediator subunit required for SREBP control of cholesterol and
RT lipid homeostasis.";
RL Nature 442:700-704(2006).
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 cholesterol-
CC dependent gene regulation. Positively regulates the Nodal signaling
CC pathway. {ECO:0000269|PubMed:12167862, ECO:0000269|PubMed:16630888,
CC ECO:0000269|PubMed:16799563}.
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 SMAD2,
CC SMAD3, SREBF1 and SREBF2. Interacts with WWTR1. Interacts with TRIM11.
CC {ECO:0000269|PubMed:10235267, ECO:0000269|PubMed:12167862,
CC ECO:0000269|PubMed:15175163, ECO:0000269|PubMed:15989967,
CC ECO:0000269|PubMed:16799563, ECO:0000269|PubMed:16904669,
CC ECO:0000269|PubMed:18568018}.
CC -!- INTERACTION:
CC Q96RN5; P42858: HTT; NbExp=3; IntAct=EBI-394506, EBI-466029;
CC Q96RN5; O60244: MED14; NbExp=2; IntAct=EBI-394506, EBI-394489;
CC Q96RN5; Q71SY5: MED25; NbExp=2; IntAct=EBI-394506, EBI-394558;
CC Q96RN5; P36956-1: SREBF1; NbExp=7; IntAct=EBI-394506, EBI-948328;
CC Q96RN5; P36956-3: SREBF1; NbExp=2; IntAct=EBI-394506, EBI-948338;
CC Q96RN5; Q12772: SREBF2; NbExp=2; IntAct=EBI-394506, EBI-465059;
CC Q96RN5; Q96F44: TRIM11; NbExp=5; IntAct=EBI-394506, EBI-851809;
CC Q96RN5-2; P54253: ATXN1; NbExp=6; IntAct=EBI-11030807, EBI-930964;
CC Q96RN5-2; P42858: HTT; NbExp=6; IntAct=EBI-11030807, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96RN5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96RN5-2; Sequence=VSP_003922;
CC Name=3;
CC IsoId=Q96RN5-3; Sequence=VSP_013024, VSP_003922;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined, including heart,
CC brain, lung, spleen, thymus, pancreas, blood leukocyte and placenta.
CC However, the level of expression varied, with highest expression in the
CC placenta and peripheral blood and lowest in the pancreas and kidney.
CC {ECO:0000269|PubMed:11024300}.
CC -!- INDUCTION: By 12-O-tetradecanoylphorbol-13-acetate (TPA).
CC {ECO:0000269|PubMed:11024300}.
CC -!- PTM: Ubiquitinated by TRIM11, leading to proteasomal degradation.
CC {ECO:0000269|PubMed:16904669}.
CC -!- POLYMORPHISM: The poly-Gln region from amino acids 235-262 of PCQAP is
CC polymorphic. There are from 15 to 18 repeats in the Italian population.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 15 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC12944.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB85034.1; Type=Miscellaneous discrepancy; Note=Several sequencing errors.; Evidence={ECO:0000305};
CC Sequence=BAC03446.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF056191; AAC12944.1; ALT_FRAME; mRNA.
DR EMBL; AF328769; AAK58423.1; -; mRNA.
DR EMBL; AK074268; BAB85034.1; ALT_SEQ; mRNA.
DR EMBL; AK090465; BAC03446.1; ALT_INIT; mRNA.
DR EMBL; CR456537; CAG30423.1; -; mRNA.
DR EMBL; CH471176; EAX02951.1; -; Genomic_DNA.
DR EMBL; CH471176; EAX02952.1; -; Genomic_DNA.
DR EMBL; CH471176; EAX02954.1; -; Genomic_DNA.
DR EMBL; CH471176; EAX02956.1; -; Genomic_DNA.
DR EMBL; BC007529; AAH07529.1; -; mRNA.
DR EMBL; BC013985; AAH13985.1; -; mRNA.
DR EMBL; U80745; AAB91443.1; -; mRNA.
DR CCDS; CCDS13781.1; -. [Q96RN5-2]
DR CCDS; CCDS33602.1; -. [Q96RN5-1]
DR CCDS; CCDS74824.1; -. [Q96RN5-3]
DR RefSeq; NP_001003891.1; NM_001003891.2. [Q96RN5-1]
DR RefSeq; NP_001280164.1; NM_001293235.1.
DR RefSeq; NP_001280165.1; NM_001293236.1. [Q96RN5-3]
DR RefSeq; NP_056973.2; NM_015889.4. [Q96RN5-2]
DR PDB; 2GUT; NMR; -; A=5-78.
DR PDB; 7EMF; EM; 3.50 A; O=1-788.
DR PDB; 7ENA; EM; 4.07 A; o=1-788.
DR PDB; 7ENC; EM; 4.13 A; o=1-788.
DR PDB; 7ENJ; EM; 4.40 A; O=1-788.
DR PDB; 7LBM; EM; 4.80 A; z=1-788.
DR PDBsum; 2GUT; -.
DR PDBsum; 7EMF; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7ENJ; -.
DR PDBsum; 7LBM; -.
DR AlphaFoldDB; Q96RN5; -.
DR BMRB; Q96RN5; -.
DR SMR; Q96RN5; -.
DR BioGRID; 119623; 113.
DR ComplexPortal; CPX-3227; Core mediator complex.
DR CORUM; Q96RN5; -.
DR DIP; DIP-32908N; -.
DR IntAct; Q96RN5; 55.
DR MINT; Q96RN5; -.
DR STRING; 9606.ENSP00000263205; -.
DR GlyGen; Q96RN5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96RN5; -.
DR PhosphoSitePlus; Q96RN5; -.
DR BioMuta; MED15; -.
DR DMDM; 27734440; -.
DR EPD; Q96RN5; -.
DR jPOST; Q96RN5; -.
DR MassIVE; Q96RN5; -.
DR MaxQB; Q96RN5; -.
DR PaxDb; Q96RN5; -.
DR PeptideAtlas; Q96RN5; -.
DR PRIDE; Q96RN5; -.
DR ProteomicsDB; 77993; -. [Q96RN5-1]
DR ProteomicsDB; 77994; -. [Q96RN5-2]
DR ProteomicsDB; 77995; -. [Q96RN5-3]
DR Antibodypedia; 282; 305 antibodies from 32 providers.
DR DNASU; 51586; -.
DR Ensembl; ENST00000263205.11; ENSP00000263205.7; ENSG00000099917.17. [Q96RN5-1]
DR Ensembl; ENST00000292733.11; ENSP00000292733.7; ENSG00000099917.17. [Q96RN5-2]
DR Ensembl; ENST00000382974.6; ENSP00000372434.2; ENSG00000099917.17. [Q96RN5-3]
DR GeneID; 51586; -.
DR KEGG; hsa:51586; -.
DR MANE-Select; ENST00000263205.11; ENSP00000263205.7; NM_001003891.3; NP_001003891.1.
DR UCSC; uc002zsp.4; human. [Q96RN5-1]
DR CTD; 51586; -.
DR DisGeNET; 51586; -.
DR GeneCards; MED15; -.
DR HGNC; HGNC:14248; MED15.
DR HPA; ENSG00000099917; Low tissue specificity.
DR MIM; 607372; gene.
DR neXtProt; NX_Q96RN5; -.
DR OpenTargets; ENSG00000099917; -.
DR PharmGKB; PA33088; -.
DR VEuPathDB; HostDB:ENSG00000099917; -.
DR eggNOG; KOG4274; Eukaryota.
DR GeneTree; ENSGT00730000111140; -.
DR HOGENOM; CLU_023921_0_0_1; -.
DR InParanoid; Q96RN5; -.
DR OMA; CCLDDKR; -.
DR PhylomeDB; Q96RN5; -.
DR TreeFam; TF324988; -.
DR PathwayCommons; Q96RN5; -.
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; Q96RN5; -.
DR SIGNOR; Q96RN5; -.
DR BioGRID-ORCS; 51586; 126 hits in 1098 CRISPR screens.
DR ChiTaRS; MED15; human.
DR EvolutionaryTrace; Q96RN5; -.
DR GeneWiki; MED15; -.
DR GenomeRNAi; 51586; -.
DR Pharos; Q96RN5; Tbio.
DR PRO; PR:Q96RN5; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q96RN5; protein.
DR Bgee; ENSG00000099917; Expressed in sural nerve and 191 other tissues.
DR ExpressionAtlas; Q96RN5; baseline and differential.
DR Genevisible; Q96RN5; HS.
DR GO; GO:0070847; C:core mediator complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016592; C:mediator complex; IEA:InterPro.
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:0003712; F:transcription coregulator activity; IEA:InterPro.
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:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR Gene3D; 1.10.246.20; -; 1.
DR InterPro; IPR036529; KIX_dom_sf.
DR InterPro; IPR019087; Med15.
DR Pfam; PF09606; Med15; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Triplet repeat expansion; Ubl conjugation.
FT CHAIN 1..788
FT /note="Mediator of RNA polymerase II transcription subunit
FT 15"
FT /id="PRO_0000058264"
FT REGION 9..73
FT /note="Interaction with SREBF1"
FT /evidence="ECO:0000269|PubMed:16799563"
FT REGION 95..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 547..564
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 271..285
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..315
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..461
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..491
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 349
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q924H2"
FT MOD_RES 603
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 80..151
FT /note="DPMNALQSLTGGPAAGAAGIGMPPRGPGQSLGGMGSLGAMGQPMSLSGQPPP
FT GTSGMAPHSMAVVSTATPQT -> A (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15461802"
FT /id="VSP_013024"
FT VAR_SEQ 385..424
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11024300,
FT ECO:0000303|PubMed:11414760, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15461802, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9225980"
FT /id="VSP_003922"
FT VARIANT 261..262
FT /note="Missing"
FT /id="VAR_013136"
FT MUTAGEN 42
FT /note="E->A: Abrogates interaction with SREBF1."
FT /evidence="ECO:0000269|PubMed:16799563"
FT MUTAGEN 58
FT /note="L->D: Abrogates interaction with SREBF1."
FT /evidence="ECO:0000269|PubMed:16799563"
FT MUTAGEN 60
FT /note="A->D: Abrogates interaction with SREBF1."
FT /evidence="ECO:0000269|PubMed:16799563"
FT CONFLICT 12
FT /note="S -> R (in Ref. 1; AAC12944)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="L -> F (in Ref. 1; AAC12944)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="Q -> H (in Ref. 3; BAC03446)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="Q -> R (in Ref. 3; BAB85034)"
FT /evidence="ECO:0000305"
FT CONFLICT 185..186
FT /note="QQ -> EL (in Ref. 7; AAB91443)"
FT /evidence="ECO:0000305"
FT CONFLICT 186..187
FT /note="Missing (in Ref. 4; CAG30423)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="Missing (in Ref. 4; CAG30423)"
FT /evidence="ECO:0000305"
FT CONFLICT 232..287
FT /note="Missing (in Ref. 3; BAB85034)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="Q -> E (in Ref. 1; AAC12944 and 7; AAB91443)"
FT /evidence="ECO:0000305"
FT CONFLICT 572..573
FT /note="IL -> GI (in Ref. 7; AAB91443)"
FT /evidence="ECO:0000305"
FT CONFLICT 685
FT /note="L -> V (in Ref. 3; BAB85034)"
FT /evidence="ECO:0000305"
FT HELIX 13..30
FT /evidence="ECO:0007829|PDB:2GUT"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:2GUT"
FT HELIX 52..71
FT /evidence="ECO:0007829|PDB:2GUT"
FT TURN 616..618
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 619..627
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 634..649
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 676..683
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 695..697
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 700..707
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 713..715
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 722..725
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 735..737
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 740..743
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 747..761
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 769..787
FT /evidence="ECO:0007829|PDB:7EMF"
SQ SEQUENCE 788 AA; 86753 MW; BB6AC6C63ED2F97E CRC64;
MDVSGQETDW RSTAFRQKLV SQIEDAMRKA GVAHSKSSKD MESHVFLKAK TRDEYLSLVA
RLIIHFRDIH NKKSQASVSD PMNALQSLTG GPAAGAAGIG MPPRGPGQSL GGMGSLGAMG
QPMSLSGQPP PGTSGMAPHS MAVVSTATPQ TQLQLQQVAL QQQQQQQQFQ QQQQAALQQQ
QQQQQQQQFQ AQQSAMQQQF QAVVQQQQQL QQQQQQQQHL IKLHHQNQQQ IQQQQQQLQR
IAQLQLQQQQ QQQQQQQQQQ QQALQAQPPI QQPPMQQPQP PPSQALPQQL QQMHHTQHHQ
PPPQPQQPPV AQNQPSQLPP QSQTQPLVSQ AQALPGQMLY TQPPLKFVRA PMVVQQPPVQ
PQVQQQQTAV QTAQAAQMVA PGVQMITEAL AQGGMHIRAR FPPTTAVSAI PSSSIPLGRQ
PMAQVSQSSL PMLSSPSPGQ QVQTPQSMPP PPQPSPQPGQ PSSQPNSNVS SGPAPSPSSF
LPSPSPQPSQ SPVTARTPQN FSVPSPGPLN TPVNPSSVMS PAGSSQAEEQ QYLDKLKQLS
KYIEPLRRMI NKIDKNEDRK KDLSKMKSLL DILTDPSKRC PLKTLQKCEI ALEKLKNDMA
VPTPPPPPVP PTKQQYLCQP LLDAVLANIR SPVFNHSLYR TFVPAMTAIH GPPITAPVVC
TRKRRLEDDE RQSIPSVLQG EVARLDPKFL VNLDPSHCSN NGTVHLICKL DDKDLPSVPP
LELSVPADYP AQSPLWIDRQ WQYDANPFLQ SVHRCMTSRL LQLPDKHSVT ALLNTWAQSV
HQACLSAA
