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Mediator of RNA polymerase II transcription subunit 24 (Mediator complex subunit 24) (Thyroid hormone receptor-associated protein 4) (Thyroid hormone receptor-associated protein complex 100 kDa component) (Trap100) (mTRAP100)

 MED24_MOUSE             Reviewed;         987 AA.
Q99K74; A3KFP0; Q8R004; Q9D277; Q9WVF1;
02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
10-OCT-2018, entry version 112.
RecName: Full=Mediator of RNA polymerase II transcription subunit 24;
AltName: Full=Mediator complex subunit 24;
AltName: Full=Thyroid hormone receptor-associated protein 4;
AltName: Full=Thyroid hormone receptor-associated protein complex 100 kDa component;
Short=Trap100;
Short=mTRAP100;
Name=Med24; Synonyms=D11Ertd307e, Thrap4, Trap100;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH
MED1, AND TISSUE SPECIFICITY.
PubMed=10406464; DOI=10.1210/mend.13.7.0295;
Zhang J., Fondell J.D.;
"Identification of mouse TRAP100: a transcriptional coregulatory
factor for thyroid hormone and vitamin D receptors.";
Mol. Endocrinol. 13:1130-1140(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=ILS, and ISS;
PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
"High-throughput sequence identification of gene coding variants
within alcohol-related QTLs.";
Mamm. Genome 12:657-663(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
STRAIN=C57BL/6J, and NOD; TISSUE=Cecum, and Dendritic cell;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, INTERACTION WITH MED10, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
PubMed=12093747; DOI=10.1093/emboj/cdf348;
Ito M., Okano H.J., Darnell R.B., Roeder R.G.;
"The TRAP100 component of the TRAP/Mediator complex is essential in
broad transcriptional events and development.";
EMBO J. 21:3464-3475(2002).
[7]
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C3H/HeJ;
PubMed=11934987; DOI=10.1126/science.1068943;
Stevens J.L., Cantin G.T., Wang G., Shevchenko A., Shevchenko A.,
Berk A.J.;
"Transcription control by E1A and MAP kinase pathway via Sur2 mediator
subunit.";
Science 296:755-758(2002).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-860, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-860 AND SER-871, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Component of the Mediator complex, a coactivator
involved in the regulated transcription of nearly all RNA
polymerase II-dependent genes. Mediator functions as a bridge to
convey information from gene-specific regulatory proteins to the
basal RNA polymerase II transcription machinery. Mediator is
recruited to promoters by direct interactions with regulatory
proteins and serves as a scaffold for the assembly of a functional
preinitiation complex with RNA polymerase II and the general
transcription factors (By similarity). Required for basal and
activator-dependent transcription. {ECO:0000250,
ECO:0000269|PubMed:10406464, ECO:0000269|PubMed:12093747}.
-!- SUBUNIT: Component of the Mediator complex, which is composed of
MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13,
MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21,
MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31,
CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8
subunits form a distinct module termed the CDK8 module. Mediator
containing the CDK8 module is less active than Mediator lacking
this module in supporting transcriptional activation. Individual
preparations of the Mediator complex lacking one or more distinct
subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and
TRAP. Interacts with AR (By similarity). Interacts with MED1 and
MED10. {ECO:0000250, ECO:0000269|PubMed:10406464,
ECO:0000269|PubMed:12093747}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q99K74-1; Sequence=Displayed;
Name=2;
IsoId=Q99K74-2; Sequence=VSP_028355, VSP_028356;
Name=3;
IsoId=Q99K74-3; Sequence=VSP_028357, VSP_028358;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in the adrenal gland, brain,
epididymis, heart, kidney, liver, ovary, pancreas, prostate,
skeletal muscle, small intestine, spleen, stomach, testis and
thymus. {ECO:0000269|PubMed:10406464,
ECO:0000269|PubMed:12093747}.
-!- DEVELOPMENTAL STAGE: Expressed throughout development; expression
levels drop immediately after birth. Strongly expressed throughout
the primitive nervous system, the hepatic primoridium and the
earliest limb buds. {ECO:0000269|PubMed:12093747}.
-!- SIMILARITY: Belongs to the Mediator complex subunit 24 family.
{ECO:0000305}.
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EMBL; AF126543; AAD42776.1; -; mRNA.
EMBL; AF483498; AAL90772.1; -; mRNA.
EMBL; AF483499; AAL90773.1; -; mRNA.
EMBL; AK020269; BAB32051.1; -; mRNA.
EMBL; AK154618; BAE32717.1; -; mRNA.
EMBL; AL590963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC005409; AAH05409.1; -; mRNA.
CCDS; CCDS25361.2; -. [Q99K74-1]
RefSeq; NP_035999.2; NM_011869.2. [Q99K74-1]
RefSeq; XP_006533368.1; XM_006533305.2.
UniGene; Mm.246493; -.
ProteinModelPortal; Q99K74; -.
SMR; Q99K74; -.
BioGrid; 204840; 2.
ComplexPortal; CPX-3264; Core mediator complex.
CORUM; Q99K74; -.
IntAct; Q99K74; 4.
MINT; Q99K74; -.
STRING; 10090.ENSMUSP00000017354; -.
iPTMnet; Q99K74; -.
PhosphoSitePlus; Q99K74; -.
EPD; Q99K74; -.
PaxDb; Q99K74; -.
PeptideAtlas; Q99K74; -.
PRIDE; Q99K74; -.
Ensembl; ENSMUST00000017354; ENSMUSP00000017354; ENSMUSG00000017210. [Q99K74-1]
GeneID; 23989; -.
KEGG; mmu:23989; -.
UCSC; uc007lgz.1; mouse. [Q99K74-2]
UCSC; uc007lha.1; mouse. [Q99K74-1]
UCSC; uc007lhc.1; mouse. [Q99K74-3]
CTD; 9862; -.
MGI; MGI:1344385; Med24.
eggNOG; ENOG410IF72; Eukaryota.
eggNOG; ENOG410YPDT; LUCA.
GeneTree; ENSGT00390000016438; -.
HOGENOM; HOG000293419; -.
HOVERGEN; HBG055588; -.
InParanoid; Q99K74; -.
KO; K15167; -.
PhylomeDB; Q99K74; -.
TreeFam; TF323565; -.
Reactome; R-MMU-212436; Generic Transcription Pathway.
ChiTaRS; Med24; mouse.
PRO; PR:Q99K74; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000017210; Expressed in 260 organ(s), highest expression level in cerebral cortex.
CleanEx; MM_MED24; -.
ExpressionAtlas; Q99K74; baseline and differential.
GO; GO:0016592; C:mediator complex; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
GO; GO:0004402; F:histone acetyltransferase activity; ISO:MGI.
GO; GO:0038023; F:signaling receptor activity; ISO:MGI.
GO; GO:0046966; F:thyroid hormone receptor binding; ISO:MGI.
GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
GO; GO:0003712; F:transcription coregulator activity; ISO:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
GO; GO:0030521; P:androgen receptor signaling pathway; ISO:MGI.
GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0051291; P:protein heterooligomerization; ISO:MGI.
GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISO:MGI.
InterPro; IPR021429; Mediator_Med24_N.
Pfam; PF11277; Med24_N; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation.
CHAIN 1 987 Mediator of RNA polymerase II
transcription subunit 24.
/FTId=PRO_0000305912.
MOTIF 128 132 LXXLL motif 1.
MOTIF 344 348 LXXLL motif 2.
MOTIF 446 450 LXXLL motif 3.
MOTIF 555 559 LXXLL motif 4.
MOTIF 786 790 LXXLL motif 5.
MOTIF 855 859 LXXLL motif 6.
MOD_RES 860 860 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 871 871 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 50 Missing (in isoform 2).
{ECO:0000303|PubMed:10406464,
ECO:0000303|PubMed:11471062}.
/FTId=VSP_028355.
VAR_SEQ 187 187 S -> SLHTSQGLGQGGTRANQPTA (in isoform 2).
{ECO:0000303|PubMed:10406464,
ECO:0000303|PubMed:11471062}.
/FTId=VSP_028356.
VAR_SEQ 661 758 VVIMNSILEHMCADVLQQTATQIKFPSTGVDTMPYWNLLPP
KRPIKEVLTDIFAKVLEKGWVDSRSIHILDTLLHMGGVYWF
CNNLIKELLKETRKEH -> SVPRPRQVCGRESAPPGTNIP
PHALGLRFPGSRSATTSSSIQAPTSPPCLAAEAVHIQGSWT
LAPSFAFPYHSLAFLVTHSLSWLSRCLVCVSVSRGF (in
isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_028357.
VAR_SEQ 759 987 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_028358.
CONFLICT 26 26 N -> K (in Ref. 3; BAB32051).
{ECO:0000305}.
CONFLICT 503 503 Q -> H (in Ref. 1; AAD42776).
{ECO:0000305}.
CONFLICT 541 541 D -> E (in Ref. 1; AAD42776).
{ECO:0000305}.
CONFLICT 566 566 K -> N (in Ref. 1; AAD42776).
{ECO:0000305}.
CONFLICT 608 608 K -> N (in Ref. 1; AAD42776).
{ECO:0000305}.
CONFLICT 699 699 L -> F (in Ref. 1; AAD42776).
{ECO:0000305}.
CONFLICT 888 888 T -> R (in Ref. 1; AAD42776).
{ECO:0000305}.
CONFLICT 940 940 S -> T (in Ref. 1; AAD42776).
{ECO:0000305}.
CONFLICT 963 963 K -> E (in Ref. 1; AAD42776).
{ECO:0000305}.
CONFLICT 970 970 D -> H (in Ref. 1; AAD42776).
{ECO:0000305}.
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


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