Entry euk: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   10-MAY-2017, entry version 158.
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;
GN   Synonyms=ARC100, CRSP4, DRIP100, KIAA0130, THRAP4, TRAP100;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   protein (TRAP) coactivator complex interacts directly with nuclear
RT   receptors in a 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
RP   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
RT   in a ligand-dependent manner and enhances VDR transactivation in a
RT   cell-free system.";
RL   Genes Dev. 12:1787-1800(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP   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.
RT   The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
RT   analysis of 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   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
RT   the 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
RT   project: 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
RP   COMPLEX.
RX   PubMed=10235267; DOI=10.1038/19789;
RA   Naeaer A.M., Beaurang P.A., Zhou S., Abraham S., Solomon W.B.,
RA   Tjian R.;
RT   "Composite co-activator ARC mediates chromatin-directed
RT   transcriptional 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.,
RA   Naeaer A.M., Erdjument-Bromage H., Tempst P., Freedman L.P.;
RT   "Ligand-dependent transcription activation by nuclear receptors
RT   requires 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.,
RA   Martinez E., 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.
RA   Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X.,
RA   Martinez E., 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
RT   receptor-mediated gene expression.";
RL   J. Biol. Chem. 277:42852-42858(2002).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP   MEDIATOR 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.,
RA   Conaway J.W., 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
RP   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   [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
RT   recruitment of transcription factor IIB during preinitiation complex
RT   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
RT   the 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.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a 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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome 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
CC       involved in the regulated transcription of nearly all RNA
CC       polymerase II-dependent genes. Mediator functions as a bridge to
CC       convey information from gene-specific regulatory proteins to the
CC       basal RNA polymerase II transcription machinery. Mediator is
CC       recruited to promoters by direct interactions with regulatory
CC       proteins and serves as a scaffold for the assembly of a functional
CC       preinitiation complex with RNA polymerase II and the general
CC       transcription factors. {ECO:0000269|PubMed:12218053,
CC       ECO:0000269|PubMed:16595664}.
CC   -!- SUBUNIT: Component of the Mediator complex, which is composed of
CC       MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13,
CC       MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21,
CC       MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31,
CC       CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8
CC       subunits form a distinct module termed the CDK8 module. Mediator
CC       containing the CDK8 module is less active than Mediator lacking
CC       this module in supporting transcriptional activation. Individual
CC       preparations of the Mediator complex lacking one or more distinct
CC       subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and
CC       TRAP. Interacts with AR. {ECO:0000269|PubMed:10024883,
CC       ECO:0000269|PubMed:10235266, ECO:0000269|PubMed:10235267,
CC       ECO:0000269|PubMed:12218053, ECO:0000269|PubMed:15175163,
CC       ECO:0000269|PubMed:15989967, ECO:0000269|PubMed:16595664,
CC       ECO:0000269|PubMed:9637681}.
CC   -!- INTERACTION:
CC       Q9Y2X0:MED16; NbExp=2; IntAct=EBI-394523, EBI-394541;
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
CC       and 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. [O75448-1]
DR   UniGene; Hs.462983; -.
DR   ProteinModelPortal; O75448; -.
DR   BioGrid; 115196; 77.
DR   DIP; DIP-31462N; -.
DR   IntAct; O75448; 36.
DR   MINT; MINT-244199; -.
DR   STRING; 9606.ENSP00000377686; -.
DR   iPTMnet; O75448; -.
DR   PhosphoSitePlus; O75448; -.
DR   BioMuta; MED24; -.
DR   EPD; O75448; -.
DR   MaxQB; O75448; -.
DR   PaxDb; O75448; -.
DR   PeptideAtlas; O75448; -.
DR   PRIDE; O75448; -.
DR   DNASU; 9862; -.
DR   Ensembl; ENST00000356271; ENSP00000348610; ENSG00000008838. [O75448-2]
DR   Ensembl; ENST00000394127; ENSP00000377685; ENSG00000008838. [O75448-2]
DR   Ensembl; ENST00000394128; ENSP00000377686; ENSG00000008838. [O75448-1]
DR   GeneID; 9862; -.
DR   KEGG; hsa:9862; -.
DR   UCSC; uc002htt.4; human. [O75448-1]
DR   CTD; 9862; -.
DR   DisGeNET; 9862; -.
DR   GeneCards; MED24; -.
DR   GeneCards; MIR6884; -.
DR   H-InvDB; HIX0174136; -.
DR   HGNC; HGNC:22963; MED24.
DR   MIM; 607000; gene.
DR   neXtProt; NX_O75448; -.
DR   OpenTargets; ENSG00000008838; -.
DR   PharmGKB; PA162395566; -.
DR   eggNOG; ENOG410IF72; Eukaryota.
DR   eggNOG; ENOG410YPDT; LUCA.
DR   GeneTree; ENSGT00390000016438; -.
DR   HOGENOM; HOG000293419; -.
DR   HOVERGEN; HBG055588; -.
DR   InParanoid; O75448; -.
DR   KO; K15167; -.
DR   PhylomeDB; O75448; -.
DR   TreeFam; TF323565; -.
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   ChiTaRS; MED24; human.
DR   GeneWiki; MED24; -.
DR   GenomeRNAi; 9862; -.
DR   PRO; PR:O75448; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000008838; -.
DR   CleanEx; HS_MED24; -.
DR   ExpressionAtlas; O75448; baseline and differential.
DR   Genevisible; O75448; HS.
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:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; NAS:UniProtKB.
DR   GO; GO:0004872; F:receptor activity; IDA:UniProtKB.
DR   GO; GO:0001104; F:RNA polymerase II transcription cofactor activity; IDA:UniProtKB.
DR   GO; GO:0046966; F:thyroid hormone receptor binding; IDA:UniProtKB.
DR   GO; GO:0003712; F:transcription cofactor activity; IDA:UniProtKB.
DR   GO; GO:0042809; F:vitamin D receptor binding; NAS:UniProtKB.
DR   GO; GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
DR   InterPro; IPR021429; Mediator_Med24_N.
DR   Pfam; PF11277; Med24_N; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Complete proteome;
KW   Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Repeat; Transcription; Transcription regulation.
FT   CHAIN         1    989       Mediator of RNA polymerase II
FT                                transcription subunit 24.
FT                                /FTId=PRO_0000065582.
FT   MOTIF       128    132       LXXLL motif 1.
FT   MOTIF       344    348       LXXLL motif 2.
FT   MOTIF       448    452       LXXLL motif 3.
FT   MOTIF       557    561       LXXLL motif 4.
FT   MOTIF       788    792       LXXLL motif 5.
FT   MOTIF       857    861       LXXLL motif 6.
FT   MOD_RES     862    862       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     873    873       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   VAR_SEQ      72     84       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_041125.
FT   VARIANT     204    204       A -> T (in dbSNP:rs34585432).
FT                                {ECO:0000269|PubMed:8590280}.
FT                                /FTId=VAR_053969.
FT   CONFLICT     20     20       D -> Y (in Ref. 3; BAA09479).
FT                                {ECO:0000305}.
FT   CONFLICT    476    476       Missing (in Ref. 8; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    555    555       E -> G (in Ref. 2; AAF78764).
FT                                {ECO:0000305}.
FT   CONFLICT    710    710       V -> E (in Ref. 4; BAG51081).
FT                                {ECO:0000305}.
FT   CONFLICT    741    741       V -> A (in Ref. 4; BAG51081).
FT                                {ECO:0000305}.
FT   CONFLICT    969    969       A -> P (in Ref. 4; BAG51081).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         1    987       ipfam:Med24_N [T]
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
//