Entry sw:MED24_MOUSE

ID   MED24_MOUSE             Reviewed;         987 AA.
AC   Q99K74; A3KFP0; Q8R004; Q9D277; Q9WVF1;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   18-JAN-2017, entry version 102.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 24;
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=mTRAP100;
GN   Name=Med24; Synonyms=D11Ertd307e, Thrap4, Trap100;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH
RP   MED1, AND TISSUE SPECIFICITY.
RX   PubMed=10406464; DOI=10.1210/mend.13.7.0295;
RA   Zhang J., Fondell J.D.;
RT   "Identification of mouse TRAP100: a transcriptional coregulatory
RT   factor for thyroid hormone and vitamin D receptors.";
RL   Mol. Endocrinol. 13:1130-1140(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=ILS, and ISS;
RX   PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cecum, and Dendritic cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [6]
RP   FUNCTION, INTERACTION WITH MED10, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=12093747; DOI=10.1093/emboj/cdf348;
RA   Ito M., Okano H.J., Darnell R.B., Roeder R.G.;
RT   "The TRAP100 component of the TRAP/Mediator complex is essential in
RT   broad transcriptional events and development.";
RL   EMBO J. 21:3464-3475(2002).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C3H/HeJ;
RX   PubMed=11934987; DOI=10.1126/science.1068943;
RA   Stevens J.L., Cantin G.T., Wang G., Shevchenko A., Shevchenko A.,
RA   Berk A.J.;
RT   "Transcription control by E1A and MAP kinase pathway via Sur2 mediator
RT   subunit.";
RL   Science 296:755-758(2002).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-860, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-860 AND SER-871, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
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 (By similarity). Required for basal and
CC       activator-dependent transcription. {ECO:0000250,
CC       ECO:0000269|PubMed:10406464, ECO:0000269|PubMed:12093747}.
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 (By similarity). Interacts with MED1 and
CC       MED10. {ECO:0000250, ECO:0000269|PubMed:10406464,
CC       ECO:0000269|PubMed:12093747}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q99K74-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99K74-2; Sequence=VSP_028355, VSP_028356;
CC       Name=3;
CC         IsoId=Q99K74-3; Sequence=VSP_028357, VSP_028358;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Expressed in the adrenal gland, brain,
CC       epididymis, heart, kidney, liver, ovary, pancreas, prostate,
CC       skeletal muscle, small intestine, spleen, stomach, testis and
CC       thymus. {ECO:0000269|PubMed:10406464,
CC       ECO:0000269|PubMed:12093747}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development; expression
CC       levels drop immediately after birth. Strongly expressed throughout
CC       the primitive nervous system, the hepatic primoridium and the
CC       earliest limb buds. {ECO:0000269|PubMed:12093747}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 24 family.
CC       {ECO:0000305}.
DR   EMBL; AF126543; AAD42776.1; -; mRNA.
DR   EMBL; AF483498; AAL90772.1; -; mRNA.
DR   EMBL; AF483499; AAL90773.1; -; mRNA.
DR   EMBL; AK020269; BAB32051.1; -; mRNA.
DR   EMBL; AK154618; BAE32717.1; -; mRNA.
DR   EMBL; AL590963; CAM46193.1; -; Genomic_DNA.
DR   EMBL; BC005409; AAH05409.1; -; mRNA.
DR   CCDS; CCDS25361.2; -. [Q99K74-1]
DR   RefSeq; NP_035999.2; NM_011869.2. [Q99K74-1]
DR   RefSeq; XP_006533368.1; XM_006533305.2. [Q99K74-1]
DR   UniGene; Mm.246493; -.
DR   ProteinModelPortal; Q99K74; -.
DR   SMR; Q99K74; -.
DR   BioGrid; 204840; 2.
DR   IntAct; Q99K74; 4.
DR   STRING; 10090.ENSMUSP00000017354; -.
DR   iPTMnet; Q99K74; -.
DR   PhosphoSitePlus; Q99K74; -.
DR   EPD; Q99K74; -.
DR   PaxDb; Q99K74; -.
DR   PeptideAtlas; Q99K74; -.
DR   PRIDE; Q99K74; -.
DR   Ensembl; ENSMUST00000017354; ENSMUSP00000017354; ENSMUSG00000017210. [Q99K74-1]
DR   GeneID; 23989; -.
DR   KEGG; mmu:23989; -.
DR   UCSC; uc007lgz.1; mouse. [Q99K74-2]
DR   UCSC; uc007lha.1; mouse. [Q99K74-1]
DR   UCSC; uc007lhc.1; mouse. [Q99K74-3]
DR   CTD; 9862; -.
DR   MGI; MGI:1344385; Med24.
DR   eggNOG; ENOG410IF72; Eukaryota.
DR   eggNOG; ENOG410YPDT; LUCA.
DR   GeneTree; ENSGT00390000016438; -.
DR   HOGENOM; HOG000293419; -.
DR   HOVERGEN; HBG055588; -.
DR   InParanoid; Q99K74; -.
DR   KO; K15167; -.
DR   PhylomeDB; Q99K74; -.
DR   TreeFam; TF323565; -.
DR   Reactome; R-MMU-212436; Generic Transcription Pathway.
DR   Reactome; R-MMU-381340; Transcriptional regulation of white adipocyte differentiation.
DR   Reactome; R-MMU-442533; Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
DR   ChiTaRS; Med24; mouse.
DR   PRO; PR:Q99K74; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000017210; -.
DR   CleanEx; MM_MED24; -.
DR   ExpressionAtlas; Q99K74; baseline and differential.
DR   GO; GO:0016592; C:mediator complex; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:Ensembl.
DR   GO; GO:0004872; F:receptor activity; ISO:MGI.
DR   GO; GO:0001104; F:RNA polymerase II transcription cofactor activity; ISO:MGI.
DR   GO; GO:0046966; F:thyroid hormone receptor binding; ISO:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR   GO; GO:0003712; F:transcription cofactor activity; ISO:MGI.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:0030521; P:androgen receptor signaling pathway; ISO:MGI.
DR   GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR   GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
DR   GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; IMP:MGI.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISO:MGI.
DR   InterPro; IPR021429; Mediator_Med24_N.
DR   Pfam; PF11277; Med24_N; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Complete proteome; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    987       Mediator of RNA polymerase II
FT                                transcription subunit 24.
FT                                /FTId=PRO_0000305912.
FT   MOTIF       128    132       LXXLL motif 1.
FT   MOTIF       344    348       LXXLL motif 2.
FT   MOTIF       446    450       LXXLL motif 3.
FT   MOTIF       555    559       LXXLL motif 4.
FT   MOTIF       786    790       LXXLL motif 5.
FT   MOTIF       855    859       LXXLL motif 6.
FT   MOD_RES     860    860       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES     871    871       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   VAR_SEQ       1     50       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:10406464,
FT                                ECO:0000303|PubMed:11471062}.
FT                                /FTId=VSP_028355.
FT   VAR_SEQ     187    187       S -> SLHTSQGLGQGGTRANQPTA (in isoform 2).
FT                                {ECO:0000303|PubMed:10406464,
FT                                ECO:0000303|PubMed:11471062}.
FT                                /FTId=VSP_028356.
FT   VAR_SEQ     661    758       VVIMNSILEHMCADVLQQTATQIKFPSTGVDTMPYWNLLPP
FT                                KRPIKEVLTDIFAKVLEKGWVDSRSIHILDTLLHMGGVYWF
FT                                CNNLIKELLKETRKEH -> SVPRPRQVCGRESAPPGTNIP
FT                                PHALGLRFPGSRSATTSSSIQAPTSPPCLAAEAVHIQGSWT
FT                                LAPSFAFPYHSLAFLVTHSLSWLSRCLVCVSVSRGF (in
FT                                isoform 3).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_028357.
FT   VAR_SEQ     759    987       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_028358.
FT   CONFLICT     26     26       N -> K (in Ref. 3; BAB32051).
FT                                {ECO:0000305}.
FT   CONFLICT    503    503       Q -> H (in Ref. 1; AAD42776).
FT                                {ECO:0000305}.
FT   CONFLICT    541    541       D -> E (in Ref. 1; AAD42776).
FT                                {ECO:0000305}.
FT   CONFLICT    566    566       K -> N (in Ref. 1; AAD42776).
FT                                {ECO:0000305}.
FT   CONFLICT    608    608       K -> N (in Ref. 1; AAD42776).
FT                                {ECO:0000305}.
FT   CONFLICT    699    699       L -> F (in Ref. 1; AAD42776).
FT                                {ECO:0000305}.
FT   CONFLICT    888    888       T -> R (in Ref. 1; AAD42776).
FT                                {ECO:0000305}.
FT   CONFLICT    940    940       S -> T (in Ref. 1; AAD42776).
FT                                {ECO:0000305}.
FT   CONFLICT    963    963       K -> E (in Ref. 1; AAD42776).
FT                                {ECO:0000305}.
FT   CONFLICT    970    970       D -> H (in Ref. 1; AAD42776).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         1    985       ipfam:Med24_N [T]
SQ   SEQUENCE   987 AA;  109985 MW;  713C6A02C3C0B294 CRC64;
     MKVVNLKQAI LQAWKERWSD YQWAINMKKF FPKGATWDIL NLAEALLEQA MIGPSPNPLI
     LSYLKYAISS QMVSCSSVLT AISKFDDFSR DLCVQALLDI MDMFCDRLSC HGKAEECIGL
     CRALLSALHW LLRCTAASAE RLQEGLEAGT PAPGEKQLAL CLQCLEKTLS STKNRALLHI
     AKLEEASSWT AIEHSLLKLG EILANLSNPQ LRSQAERCGT LIRSIPSMLS VHSEQLHKTG
     FPTIHALILL EGTMNLTGEM QPLVEQLMMV KRMQHIPTPL FVLEIWKACF VGLIESPEGT
     QELKWTAFTY LKIPQVLVKL KKYFHGEKDF TEDVNCAFEF LLKLTPLLDK ADQRCNCDCT
     NFLLQECNKQ GLLSEVNFAS LVGKRTADRD PQLKSSENAN IQPNPGLILR AEPTVTNILK
     TMDADHSKSP EGLLGVLGHM LSGKSLDLLL AAAAATGKLK SFARKFINLN EFTTHGSGES
     TKTASVRALL FDISFLMLCH VAQTYGSEVI LSESSSGEEV PFFETWMQTC MPEEGKILNP
     DHPCFRPDST KVESLVALLN NSSEMKLVQM KWHEACLSIS AAILEILNAW ENGVLAFESI
     QKITDNIKGK VCSLAVCAVA WLVAHVRMLG LDEREKSLQM IRQLAGPLYS ENTLQFYNER
     VVIMNSILEH MCADVLQQTA TQIKFPSTGV DTMPYWNLLP PKRPIKEVLT DIFAKVLEKG
     WVDSRSIHIL DTLLHMGGVY WFCNNLIKEL LKETRKEHTL RAVQLLYSIF CLDMQQVTLV
     LLGHILPGLL TDSSKWHSLM DPPGTALAKL AVWCALSSYS SHKGQASSRQ KKRHREDIED
     YVSLFPVEDM QPSKLMRLLS SSDDDANILS SPTDRSMNSS LSASQLHTVN MRDPLNRVLA
     NLFLLISSIL GSRTAGPHTQ FVQWFMEECV GCLEQDSRGS ILQFMPFTTV SELVKVSAMS
     SPKVVLAITD LSLPLGRQVA AKAIAAL
//