MED24_HUMAN
ID MED24_HUMAN Reviewed; 989 AA.
AC O75448; A8K4S5; B3KMR9; Q14143; Q9NNY5;
DT 24-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 24;
DE AltName: Full=Activator-recruited cofactor 100 kDa component;
DE Short=ARC100;
DE AltName: Full=Cofactor required for Sp1 transcriptional activation subunit 4;
DE Short=CRSP complex subunit 4;
DE AltName: Full=Mediator complex subunit 24;
DE AltName: Full=Thyroid hormone receptor-associated protein 4;
DE AltName: Full=Thyroid hormone receptor-associated protein complex 100 kDa component;
DE Short=Trap100;
DE Short=hTRAP100;
DE AltName: Full=Vitamin D3 receptor-interacting protein complex 100 kDa component;
DE Short=DRIP100;
GN Name=MED24; Synonyms=ARC100, CRSP4, DRIP100, KIAA0130, THRAP4, TRAP100;
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), PROTEIN SEQUENCE OF 1-15, AND
RP TISSUE SPECIFICITY.
RX PubMed=9653119; DOI=10.1073/pnas.95.14.7939;
RA Yuan C.-X., Ito M., Fondell J.D., Fu Z.-Y., Roeder R.G.;
RT "The TRAP220 component of a thyroid hormone receptor-associated protein
RT (TRAP) coactivator complex interacts directly with nuclear receptors in a
RT ligand-dependent fashion.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7939-7944(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND IDENTIFICATION IN DRIP COMPLEX.
RX PubMed=9637681; DOI=10.1101/gad.12.12.1787;
RA Rachez C., Suldan Z., Ward J., Chang C.-P.B., Burakov D.,
RA Erdjument-Bromage H., Tempst P., Freedman L.P.;
RT "A novel protein complex that interacts with the vitamin D3 receptor in a
RT ligand-dependent manner and enhances VDR transactivation in a cell-free
RT system.";
RL Genes Dev. 12:1787-1800(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-204.
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV. The
RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Teratocarcinoma;
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 GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 PROTEIN SEQUENCE OF 1-11 AND 957-965, AND IDENTIFICATION IN ARC 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 [8]
RP PROTEIN SEQUENCE OF 467-489, AND IDENTIFICATION IN ARC COMPLEX.
RC TISSUE=Cervix carcinoma;
RX PubMed=10235266; DOI=10.1038/19783;
RA Rachez C., Lemon B.D., Suldan Z., Bromleigh V., Gamble M., Naeaer A.M.,
RA Erdjument-Bromage H., Tempst P., Freedman L.P.;
RT "Ligand-dependent transcription activation by nuclear receptors requires
RT the DRIP complex.";
RL Nature 398:824-828(1999).
RN [9]
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 [10]
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 [11]
RP FUNCTION, AND INTERACTION WITH AR.
RX PubMed=12218053; DOI=10.1074/jbc.m206061200;
RA Wang Q., Sharma D., Ren Y., Fondell J.D.;
RT "A coregulatory role for the TRAP-mediator complex in androgen receptor-
RT mediated gene expression.";
RL J. Biol. Chem. 277:42852-42858(2002).
RN [12]
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 [13]
RP INTERACTION WITH MED1; MED10; 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 [14]
RP FUNCTION, AND INTERACTION WITH MED1 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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862 AND SER-873, AND
RP IDENTIFICATION BY 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 [17]
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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862 AND SER-873, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862 AND SER-873, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862 AND SER-873, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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).
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:12218053,
CC 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 AR.
CC {ECO:0000269|PubMed:10024883, ECO:0000269|PubMed:10235266,
CC ECO:0000269|PubMed:10235267, ECO:0000269|PubMed:12218053,
CC ECO:0000269|PubMed:15175163, ECO:0000269|PubMed:15989967,
CC ECO:0000269|PubMed:16595664, ECO:0000269|PubMed:9637681}.
CC -!- INTERACTION:
CC O75448; Q9Y2X0: MED16; NbExp=2; IntAct=EBI-394523, EBI-394541;
CC O75448; Q71SY5: MED25; NbExp=2; IntAct=EBI-394523, EBI-394558;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75448-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75448-2; Sequence=VSP_041125;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Abundant in skeletal muscle, heart and
CC placenta. {ECO:0000269|PubMed:9653119}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 24 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09479.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF055995; AAC39855.1; -; mRNA.
DR EMBL; AF277379; AAF78764.1; -; mRNA.
DR EMBL; D50920; BAA09479.2; ALT_INIT; mRNA.
DR EMBL; AK022508; BAG51081.1; -; mRNA.
DR EMBL; AK291040; BAF83729.1; -; mRNA.
DR EMBL; AC090844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC102799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011375; AAH11375.1; -; mRNA.
DR CCDS; CCDS11359.1; -. [O75448-1]
DR CCDS; CCDS42315.1; -. [O75448-2]
DR RefSeq; NP_001072986.1; NM_001079518.1. [O75448-2]
DR RefSeq; NP_001254726.1; NM_001267797.1. [O75448-2]
DR RefSeq; NP_055630.2; NM_014815.3. [O75448-1]
DR RefSeq; XP_016880955.1; XM_017025466.1.
DR PDB; 7EMF; EM; 3.50 A; X=1-989.
DR PDB; 7ENA; EM; 4.07 A; x=1-989.
DR PDB; 7ENC; EM; 4.13 A; x=1-989.
DR PDB; 7ENJ; EM; 4.40 A; X=1-989.
DR PDB; 7LBM; EM; 4.80 A; 2=1-989.
DR PDBsum; 7EMF; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7ENJ; -.
DR PDBsum; 7LBM; -.
DR AlphaFoldDB; O75448; -.
DR SMR; O75448; -.
DR BioGRID; 115196; 120.
DR ComplexPortal; CPX-3227; Core mediator complex.
DR CORUM; O75448; -.
DR DIP; DIP-31462N; -.
DR IntAct; O75448; 55.
DR MINT; O75448; -.
DR STRING; 9606.ENSP00000377686; -.
DR iPTMnet; O75448; -.
DR PhosphoSitePlus; O75448; -.
DR BioMuta; MED24; -.
DR CPTAC; CPTAC-933; -.
DR EPD; O75448; -.
DR jPOST; O75448; -.
DR MassIVE; O75448; -.
DR MaxQB; O75448; -.
DR PaxDb; O75448; -.
DR PeptideAtlas; O75448; -.
DR PRIDE; O75448; -.
DR ProteomicsDB; 50015; -. [O75448-1]
DR ProteomicsDB; 50016; -. [O75448-2]
DR Antibodypedia; 28479; 154 antibodies from 24 providers.
DR DNASU; 9862; -.
DR Ensembl; ENST00000356271.7; ENSP00000348610.3; ENSG00000008838.21. [O75448-2]
DR Ensembl; ENST00000394127.6; ENSP00000377685.2; ENSG00000008838.21. [O75448-2]
DR Ensembl; ENST00000394128.7; ENSP00000377686.2; ENSG00000008838.21. [O75448-1]
DR GeneID; 9862; -.
DR KEGG; hsa:9862; -.
DR MANE-Select; ENST00000394128.7; ENSP00000377686.2; NM_014815.4; NP_055630.2.
DR UCSC; uc002htt.4; human. [O75448-1]
DR CTD; 9862; -.
DR DisGeNET; 9862; -.
DR GeneCards; MED24; -.
DR HGNC; HGNC:22963; MED24.
DR HPA; ENSG00000008838; Low tissue specificity.
DR MIM; 607000; gene.
DR neXtProt; NX_O75448; -.
DR OpenTargets; ENSG00000008838; -.
DR PharmGKB; PA162395566; -.
DR VEuPathDB; HostDB:ENSG00000008838; -.
DR eggNOG; ENOG502QPJD; Eukaryota.
DR GeneTree; ENSGT00390000016438; -.
DR HOGENOM; CLU_007484_0_0_1; -.
DR InParanoid; O75448; -.
DR OMA; TWQDICL; -.
DR PhylomeDB; O75448; -.
DR TreeFam; TF323565; -.
DR PathwayCommons; O75448; -.
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; O75448; -.
DR SIGNOR; O75448; -.
DR BioGRID-ORCS; 9862; 238 hits in 1108 CRISPR screens.
DR ChiTaRS; MED24; human.
DR GeneWiki; MED24; -.
DR GenomeRNAi; 9862; -.
DR Pharos; O75448; Tbio.
DR PRO; PR:O75448; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O75448; protein.
DR Bgee; ENSG00000008838; Expressed in right hemisphere of cerebellum and 179 other tissues.
DR ExpressionAtlas; O75448; baseline and differential.
DR Genevisible; O75448; HS.
DR GO; GO:0070847; C:core mediator complex; IPI:ComplexPortal.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; NAS:UniProtKB.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IDA:UniProtKB.
DR GO; GO:0042809; F:nuclear vitamin D receptor binding; NAS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
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; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR InterPro; IPR021429; Mediator_Med24.
DR PANTHER; PTHR12898; PTHR12898; 1.
DR Pfam; PF11277; Med24_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Direct protein sequencing;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..989
FT /note="Mediator of RNA polymerase II transcription subunit
FT 24"
FT /id="PRO_0000065582"
FT MOTIF 128..132
FT /note="LXXLL motif 1"
FT MOTIF 344..348
FT /note="LXXLL motif 2"
FT MOTIF 448..452
FT /note="LXXLL motif 3"
FT MOTIF 557..561
FT /note="LXXLL motif 4"
FT MOTIF 788..792
FT /note="LXXLL motif 5"
FT MOTIF 857..861
FT /note="LXXLL motif 6"
FT MOD_RES 862
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 873
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 72..84
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041125"
FT VARIANT 204
FT /note="A -> T (in dbSNP:rs34585432)"
FT /evidence="ECO:0000269|PubMed:8590280"
FT /id="VAR_053969"
FT CONFLICT 20
FT /note="D -> Y (in Ref. 3; BAA09479)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="Missing (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="E -> G (in Ref. 2; AAF78764)"
FT /evidence="ECO:0000305"
FT CONFLICT 710
FT /note="V -> E (in Ref. 4; BAG51081)"
FT /evidence="ECO:0000305"
FT CONFLICT 741
FT /note="V -> A (in Ref. 4; BAG51081)"
FT /evidence="ECO:0000305"
FT CONFLICT 969
FT /note="A -> P (in Ref. 4; BAG51081)"
FT /evidence="ECO:0000305"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 91..104
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 114..145
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 157..170
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 172..184
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 188..205
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 211..224
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 242..253
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 260..273
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 278..294
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 300..310
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 312..323
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 330..342
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 345..355
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 359..369
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 375..390
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 406..423
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 427..430
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 432..443
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 447..457
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 461..477
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 483..506
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 510..512
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 524..532
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 552..561
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 574..594
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 599..610
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 615..630
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 637..646
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 647..649
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 659..674
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 677..680
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 696..699
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 703..705
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 707..721
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 726..753
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 758..772
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 776..785
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 787..793
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 797..800
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 803..822
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 830..838
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 843..846
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 896..913
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 919..934
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 943..946
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 950..957
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 966..969
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 970..972
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 976..987
FT /evidence="ECO:0007829|PDB:7EMF"
SQ SEQUENCE 989 AA; 110305 MW; CCEDE7D4E74D890C CRC64;
MKVVNLKQAI LQAWKERWSD YQWAINMKKF FPKGATWDIL NLADALLEQA MIGPSPNPLI
LSYLKYAISS QMVSYSSVLT AISKFDDFSR DLCVQALLDI MDMFCDRLSC HGKAEECIGL
CRALLSALHW LLRCTAASAE RLREGLEAGT PAAGEKQLAM CLQRLEKTLS STKNRALLHI
AKLEEASSWT AIEHSLLKLG EILANLSNPQ LRSQAEQCGT LIRSIPTMLS VHAEQMHKTG
FPTVHAVILL EGTMNLTGET QSLVEQLTMV KRMQHIPTPL FVLEIWKACF VGLIESPEGT
EELKWTAFTF LKIPQVLVKL KKYSHGDKDF TEDVNCAFEF LLKLTPLLDK ADQRCNCDCT
NFLLQECGKQ GLLSEASVNN LMAKRKADRE HAPQQKSGEN ANIQPNIQLI LRAEPTVTNI
LKTMDADHSK SPEGLLGVLG HMLSGKSLDL LLAAAAATGK LKSFARKFIN LNEFTTYGSE
ESTKPASVRA LLFDISFLML CHVAQTYGSE VILSESRTGA EVPFFETWMQ TCMPEEGKIL
NPDHPCFRPD STKVESLVAL LNNSSEMKLV QMKWHEACLS ISAAILEILN AWENGVLAFE
SIQKITDNIK GKVCSLAVCA VAWLVAHVRM LGLDEREKSL QMIRQLAGPL FSENTLQFYN
ERVVIMNSIL ERMCADVLQQ TATQIKFPST GVDTMPYWNL LPPKRPIKEV LTDIFAKVLE
KGWVDSRSIH IFDTLLHMGG VYWFCNNLIK ELLKETRKEH TLRAVELLYS IFCLDMQQVT
LVLLGHILPG LLTDSSKWHS LMDPPGTALA KLAVWCALSS YSSHKGQAST RQKKRHREDI
EDYISLFPLD DVQPSKLMRL LSSNEDDANI LSSPTDRSMS SSLSASQLHT VNMRDPLNRV
LANLFLLISS ILGSRTAGPH TQFVQWFMEE CVDCLEQGGR GSVLQFMPFT TVSELVKVSA
MSSPKVVLAI TDLSLPLGRQ VAAKAIAAL
