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 03-AUG-2022, entry version 130.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH MED1,
RP 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 factor for
RT 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 within
RT 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, INTERACTION WITH MED10, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP 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 broad
RT 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 BY
RP 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, Pancreas,
RC 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 expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). Required for
CC basal and 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 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 (By
CC similarity). Interacts with MED1 and MED10. {ECO:0000250,
CC ECO:0000269|PubMed:10406464, 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 -!- TISSUE SPECIFICITY: Expressed in the adrenal gland, brain, epididymis,
CC heart, kidney, liver, ovary, pancreas, prostate, skeletal muscle, small
CC intestine, spleen, stomach, testis and thymus.
CC {ECO:0000269|PubMed:10406464, ECO:0000269|PubMed:12093747}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development; expression
CC levels drop immediately after birth. Strongly expressed throughout the
CC primitive nervous system, the hepatic primoridium and the earliest limb
CC buds. {ECO:0000269|PubMed:12093747}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 24 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; -; NOT_ANNOTATED_CDS; 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.
DR PDB; 6W1S; EM; 4.02 A; S=4-985.
DR PDBsum; 6W1S; -.
DR AlphaFoldDB; Q99K74; -.
DR SMR; Q99K74; -.
DR BioGRID; 204840; 5.
DR ComplexPortal; CPX-3264; Core mediator complex.
DR CORUM; Q99K74; -.
DR IntAct; Q99K74; 4.
DR MINT; Q99K74; -.
DR STRING; 10090.ENSMUSP00000017354; -.
DR iPTMnet; Q99K74; -.
DR PhosphoSitePlus; Q99K74; -.
DR EPD; Q99K74; -.
DR jPOST; Q99K74; -.
DR MaxQB; Q99K74; -.
DR PaxDb; Q99K74; -.
DR PeptideAtlas; Q99K74; -.
DR PRIDE; Q99K74; -.
DR ProteomicsDB; 295917; -. [Q99K74-1]
DR ProteomicsDB; 295918; -. [Q99K74-2]
DR ProteomicsDB; 295919; -. [Q99K74-3]
DR Antibodypedia; 28479; 154 antibodies from 24 providers.
DR DNASU; 23989; -.
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 VEuPathDB; HostDB:ENSMUSG00000017210; -.
DR eggNOG; ENOG502QPJD; Eukaryota.
DR GeneTree; ENSGT00390000016438; -.
DR HOGENOM; CLU_007484_0_0_1; -.
DR InParanoid; Q99K74; -.
DR OMA; TWQDICL; -.
DR PhylomeDB; Q99K74; -.
DR TreeFam; TF323565; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 23989; 27 hits in 74 CRISPR screens.
DR ChiTaRS; Med24; mouse.
DR PRO; PR:Q99K74; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q99K74; protein.
DR Bgee; ENSMUSG00000017210; Expressed in primary visual cortex and 225 other tissues.
DR ExpressionAtlas; Q99K74; baseline and differential.
DR GO; GO:0070847; C:core mediator complex; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0004402; F:histone acetyltransferase activity; ISO:MGI.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
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; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..987
FT /note="Mediator of RNA polymerase II transcription subunit
FT 24"
FT /id="PRO_0000305912"
FT MOTIF 128..132
FT /note="LXXLL motif 1"
FT MOTIF 344..348
FT /note="LXXLL motif 2"
FT MOTIF 446..450
FT /note="LXXLL motif 3"
FT MOTIF 555..559
FT /note="LXXLL motif 4"
FT MOTIF 786..790
FT /note="LXXLL motif 5"
FT MOTIF 855..859
FT /note="LXXLL motif 6"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 871
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..50
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10406464,
FT ECO:0000303|PubMed:11471062"
FT /id="VSP_028355"
FT VAR_SEQ 187
FT /note="S -> SLHTSQGLGQGGTRANQPTA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10406464,
FT ECO:0000303|PubMed:11471062"
FT /id="VSP_028356"
FT VAR_SEQ 661..758
FT /note="VVIMNSILEHMCADVLQQTATQIKFPSTGVDTMPYWNLLPPKRPIKEVLTDI
FT FAKVLEKGWVDSRSIHILDTLLHMGGVYWFCNNLIKELLKETRKEH -> SVPRPRQVC
FT GRESAPPGTNIPPHALGLRFPGSRSATTSSSIQAPTSPPCLAAEAVHIQGSWTLAPSFA
FT FPYHSLAFLVTHSLSWLSRCLVCVSVSRGF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028357"
FT VAR_SEQ 759..987
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028358"
FT CONFLICT 26
FT /note="N -> K (in Ref. 3; BAB32051)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="Q -> H (in Ref. 1; AAD42776)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="D -> E (in Ref. 1; AAD42776)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="K -> N (in Ref. 1; AAD42776)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="K -> N (in Ref. 1; AAD42776)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="L -> F (in Ref. 1; AAD42776)"
FT /evidence="ECO:0000305"
FT CONFLICT 888
FT /note="T -> R (in Ref. 1; AAD42776)"
FT /evidence="ECO:0000305"
FT CONFLICT 940
FT /note="S -> T (in Ref. 1; AAD42776)"
FT /evidence="ECO:0000305"
FT CONFLICT 963
FT /note="K -> E (in Ref. 1; AAD42776)"
FT /evidence="ECO:0000305"
FT CONFLICT 970
FT /note="D -> H (in Ref. 1; AAD42776)"
FT /evidence="ECO:0000305"
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
