ID MED23_HUMAN Reviewed; 1368 AA. AC Q9ULK4; B9TX55; O95403; Q5JWT3; Q5JWT4; Q6P9H6; Q9H0J2; Q9NTT9; Q9NTU0; AC Q9Y5P7; Q9Y667; DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 22-FEB-2003, sequence version 2. DT 27-MAR-2024, entry version 186. DE RecName: Full=Mediator of RNA polymerase II transcription subunit 23; DE AltName: Full=Activator-recruited cofactor 130 kDa component; DE Short=ARC130; DE AltName: Full=Cofactor required for Sp1 transcriptional activation subunit 3; DE Short=CRSP complex subunit 3; DE AltName: Full=Mediator complex subunit 23; DE AltName: Full=Protein sur-2 homolog; DE Short=hSur-2; DE AltName: Full=Transcriptional coactivator CRSP130; DE AltName: Full=Vitamin D3 receptor-interacting protein complex 130 kDa component; DE Short=DRIP130; GN Name=MED23; Synonyms=ARC130, CRSP3, DRIP130, KIAA1216, SUR2; 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 254-280; RP 1317-1326 AND 1331-1337, 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, AND INTERACTION WITH E1A RP AND CDK8. RX PubMed=10353252; DOI=10.1038/20466; RA Boyer T.G., Martin M.E.D., Lees E., Ricciardi R.P., Berk A.J.; RT "Mammalian Srb/Mediator complex is targeted by adenovirus E1A protein."; RL Nature 399:276-279(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND IDENTIFICATION IN THE CRSP RP COMPLEX. RX PubMed=9989412; DOI=10.1038/17141; RA Ryu S., Zhou S., Ladurner A.G., Tjian R.; RT "The transcriptional cofactor complex CRSP is required for activity of the RT enhancer-binding protein Sp1."; RL Nature 397:446-450(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6). RA Kivil A., Kazantseva A., Vinkel K.J.M., Sadam H., Neuman T., Palm K.; RT "Alternative splicing as a prevalent mechanism in regulating mammalian RT mediator tail subcomplex activity."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10574462; DOI=10.1093/dnares/6.5.337; RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XV. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:337-345(1999). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Placenta; 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 [10] RP IDENTIFICATION IN THE ARC COMPLEX, AND PROTEIN SEQUENCE OF 465-473 AND RP 1302-1311. 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 [11] RP INTERACTION WITH MED6. RX PubMed=10993082; DOI=10.1038/35024111; RA Akoulitchev S., Chuikov S., Reinberg D.; RT "TFIIH is negatively regulated by cdk8-containing mediator complexes."; RL Nature 407:102-106(2000). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MEDIATOR RP COMPLEX. RX PubMed=11867769; DOI=10.1073/pnas.261715899; RA Kang Y.K., Guermah M., Yuan C.-X., Roeder R.G.; RT "The TRAP/Mediator coactivator complex interacts directly with estrogen RT receptors alpha and beta through the TRAP220 subunit and directly enhances RT estrogen receptor function in vitro."; RL Proc. Natl. Acad. Sci. U.S.A. 99:2642-2647(2002). RN [13] RP FUNCTION, AND INTERACTION WITH CEBPB. RX PubMed=14759369; DOI=10.1016/s1097-2765(03)00521-5; RA Mo X., Kowenz-Leutz E., Xu H., Leutz A.; RT "Ras induces mediator complex exchange on C/EBP beta."; RL Mol. Cell 13:241-250(2004). RN [14] 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 [15] RP INTERACTION WITH MED1 AND MED10, IDENTIFICATION BY MASS SPECTROMETRY, RP IDENTIFICATION IN THE MEDIATOR COMPLEX, AND ASSOCIATION OF THE MEDIATOR RP 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 [16] RP INTERACTION WITH CDK8; CTNNB1 AND GLI3. RX PubMed=17000779; DOI=10.1128/mcb.00443-06; RA Zhou H., Kim S., Ishii S., Boyer T.G.; RT "Mediator modulates Gli3-dependent Sonic hedgehog signaling."; RL Mol. Cell. Biol. 26:8667-8682(2006). RN [17] 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 [18] 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 [19] RP INTERACTION WITH CEBPB. RX PubMed=20111005; DOI=10.1038/emboj.2010.3; RA Kowenz-Leutz E., Pless O., Dittmar G., Knoblich M., Leutz A.; RT "Crosstalk between C/EBPbeta phosphorylation, arginine methylation, and RT SWI/SNF/Mediator implies an indexing transcription factor code."; RL EMBO J. 29:1105-1115(2010). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [21] RP INVOLVEMENT IN MRT18, VARIANT MRT18 GLN-611, AND CHARACTERIZATION OF RP VARIANT MRT18 GLN-611. RX PubMed=21868677; DOI=10.1126/science.1206638; RA Hashimoto S., Boissel S., Zarhrate M., Rio M., Munnich A., Egly J.M., RA Colleaux L.; RT "MED23 mutation links intellectual disability to dysregulation of immediate RT early gene expression."; RL Science 333:1161-1163(2011). CC -!- FUNCTION: Required for transcriptional activation subsequent to the CC assembly of the pre-initiation complex (By similarity). Component of CC the Mediator complex, a coactivator involved in the regulated CC transcription of nearly all RNA polymerase II-dependent genes. Mediator CC functions as a bridge to convey information from gene-specific CC regulatory proteins to the basal RNA polymerase II transcription CC machinery. Mediator is recruited to promoters by direct interactions CC with regulatory proteins and serves as a scaffold for the assembly of a CC functional pre-initiation complex with RNA polymerase II and the CC general transcription factors. Required for transcriptional activation CC by adenovirus E1A protein. Required for ELK1-dependent transcriptional CC activation in response to activated Ras signaling. {ECO:0000250, CC ECO:0000269|PubMed:10353252, ECO:0000269|PubMed:14759369, CC ECO:0000269|PubMed:16595664}. CC -!- SUBUNIT: Interacts with ELK1 (By similarity). Component of the Mediator CC complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, CC MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, CC MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, CC MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CC CDK8 subunits form a distinct module termed the CDK8 module. Mediator CC containing the CDK8 module is less active than Mediator lacking this CC 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 CEBPB (when not methylated), CTNNB1, and GLI3. CC Interacts with the adenovirus E1A protein. CC {ECO:0000250|UniProtKB:Q80YQ2, ECO:0000269|PubMed:10235266, CC ECO:0000269|PubMed:10235267, ECO:0000269|PubMed:10353252, CC ECO:0000269|PubMed:10993082, ECO:0000269|PubMed:11867769, CC ECO:0000269|PubMed:14759369, ECO:0000269|PubMed:15175163, CC ECO:0000269|PubMed:15989967, ECO:0000269|PubMed:16595664, CC ECO:0000269|PubMed:17000779, ECO:0000269|PubMed:20111005, CC ECO:0000269|PubMed:9989412}. CC -!- INTERACTION: CC Q9ULK4; O60244: MED14; NbExp=4; IntAct=EBI-311161, EBI-394489; CC Q9ULK4; Q9Y2X0: MED16; NbExp=4; IntAct=EBI-311161, EBI-394541; CC Q9ULK4; Q71SY5: MED25; NbExp=4; IntAct=EBI-311161, EBI-394558; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Comment=Experimental confirmation may be lacking for some isoforms.; CC Name=1; CC IsoId=Q9ULK4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9ULK4-2; Sequence=VSP_004034, VSP_004036, VSP_004037; CC Name=3; CC IsoId=Q9ULK4-3; Sequence=VSP_004034, VSP_004035; CC Name=4; CC IsoId=Q9ULK4-4; Sequence=VSP_004035; CC Name=5; CC IsoId=Q9ULK4-5; Sequence=VSP_028380; CC Name=6; CC IsoId=Q9ULK4-6; Sequence=VSP_047860, VSP_047861; CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 18, CC with or without epilepsy (MRT18) [MIM:614249]: A disorder characterized CC by significantly below average general intellectual functioning CC associated with impairments in adaptive behavior and manifested during CC the developmental period. {ECO:0000269|PubMed:21868677}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the Mediator complex subunit 23 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD12724.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAD31729.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAA86530.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AF105332; AAD31729.1; ALT_FRAME; mRNA. DR EMBL; AF135022; AAD30202.1; -; mRNA. DR EMBL; AF104255; AAD12724.1; ALT_INIT; mRNA. DR EMBL; EU392526; ACB88854.1; -; mRNA. DR EMBL; AB033042; BAA86530.1; ALT_INIT; mRNA. DR EMBL; AL136776; CAB66710.1; -; mRNA. DR EMBL; AL121575; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW48052.1; -; Genomic_DNA. DR EMBL; BC060759; AAH60759.1; -; mRNA. DR CCDS; CCDS5146.1; -. [Q9ULK4-3] DR CCDS; CCDS5147.1; -. [Q9ULK4-1] DR CCDS; CCDS59039.1; -. [Q9ULK4-5] DR RefSeq; NP_001257450.1; NM_001270521.1. [Q9ULK4-4] DR RefSeq; NP_001257451.1; NM_001270522.1. [Q9ULK4-5] DR RefSeq; NP_004821.2; NM_004830.3. [Q9ULK4-1] DR RefSeq; NP_057063.2; NM_015979.3. [Q9ULK4-3] DR PDB; 6H02; X-ray; 2.80 A; A=1-1368. DR PDB; 7EMF; EM; 3.50 A; W=1-1368. DR PDB; 7ENA; EM; 4.07 A; w=1-1368. DR PDB; 7ENC; EM; 4.13 A; w=1-1368. DR PDB; 7ENJ; EM; 4.40 A; W=1-1368. DR PDB; 7LBM; EM; 4.80 A; 1=1-1368. DR PDB; 8GXQ; EM; 5.04 A; w=1-1368. DR PDB; 8GXS; EM; 4.16 A; w=1-1368. DR PDBsum; 6H02; -. DR PDBsum; 7EMF; -. DR PDBsum; 7ENA; -. DR PDBsum; 7ENC; -. DR PDBsum; 7ENJ; -. DR PDBsum; 7LBM; -. DR PDBsum; 8GXQ; -. DR PDBsum; 8GXS; -. DR AlphaFoldDB; Q9ULK4; -. DR EMDB; EMD-23255; -. DR EMDB; EMD-31191; -. DR EMDB; EMD-31204; -. DR EMDB; EMD-31207; -. DR EMDB; EMD-31211; -. DR EMDB; EMD-34359; -. DR EMDB; EMD-34360; -. DR SMR; Q9ULK4; -. DR BioGRID; 114829; 254. DR ComplexPortal; CPX-3227; Core mediator complex. DR CORUM; Q9ULK4; -. DR DIP; DIP-31461N; -. DR IntAct; Q9ULK4; 155. DR MINT; Q9ULK4; -. DR STRING; 9606.ENSP00000357047; -. DR BindingDB; Q9ULK4; -. DR ChEMBL; CHEMBL4146; -. DR GlyGen; Q9ULK4; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9ULK4; -. DR PhosphoSitePlus; Q9ULK4; -. DR SwissPalm; Q9ULK4; -. DR BioMuta; MED23; -. DR DMDM; 28558074; -. DR EPD; Q9ULK4; -. DR jPOST; Q9ULK4; -. DR MassIVE; Q9ULK4; -. DR MaxQB; Q9ULK4; -. DR PaxDb; 9606-ENSP00000357047; -. DR PeptideAtlas; Q9ULK4; -. DR ProteomicsDB; 7541; -. DR ProteomicsDB; 85057; -. [Q9ULK4-1] DR ProteomicsDB; 85058; -. [Q9ULK4-2] DR ProteomicsDB; 85059; -. [Q9ULK4-3] DR ProteomicsDB; 85060; -. [Q9ULK4-4] DR ProteomicsDB; 85061; -. [Q9ULK4-5] DR Pumba; Q9ULK4; -. DR ABCD; Q9ULK4; 1 sequenced antibody. DR Antibodypedia; 19677; 280 antibodies from 33 providers. DR DNASU; 9439; -. DR Ensembl; ENST00000354577.8; ENSP00000346588.4; ENSG00000112282.18. [Q9ULK4-3] DR Ensembl; ENST00000368053.8; ENSP00000357032.4; ENSG00000112282.18. [Q9ULK4-2] DR Ensembl; ENST00000368060.7; ENSP00000357039.3; ENSG00000112282.18. [Q9ULK4-5] DR Ensembl; ENST00000368068.8; ENSP00000357047.3; ENSG00000112282.18. [Q9ULK4-1] DR Ensembl; ENST00000539158.1; ENSP00000445072.1; ENSG00000112282.18. [Q9ULK4-6] DR GeneID; 9439; -. DR KEGG; hsa:9439; -. DR MANE-Select; ENST00000368068.8; ENSP00000357047.3; NM_004830.4; NP_004821.2. DR UCSC; uc003qcq.5; human. [Q9ULK4-1] DR AGR; HGNC:2372; -. DR CTD; 9439; -. DR DisGeNET; 9439; -. DR GeneCards; MED23; -. DR HGNC; HGNC:2372; MED23. DR HPA; ENSG00000112282; Low tissue specificity. DR MalaCards; MED23; -. DR MIM; 605042; gene. DR MIM; 614249; phenotype. DR neXtProt; NX_Q9ULK4; -. DR OpenTargets; ENSG00000112282; -. DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability. DR PharmGKB; PA162395499; -. DR VEuPathDB; HostDB:ENSG00000112282; -. DR eggNOG; KOG1883; Eukaryota. DR GeneTree; ENSGT00390000010380; -. DR HOGENOM; CLU_002773_0_0_1; -. DR InParanoid; Q9ULK4; -. DR OMA; QKHQKQR; -. DR OrthoDB; 2899461at2759; -. DR PhylomeDB; Q9ULK4; -. DR TreeFam; TF324163; -. DR PathwayCommons; Q9ULK4; -. 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; Q9ULK4; -. DR SIGNOR; Q9ULK4; -. DR BioGRID-ORCS; 9439; 181 hits in 1192 CRISPR screens. DR ChiTaRS; MED23; human. DR GeneWiki; CRSP3; -. DR GenomeRNAi; 9439; -. DR Pharos; Q9ULK4; Tbio. DR PRO; PR:Q9ULK4; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q9ULK4; Protein. DR Bgee; ENSG00000112282; Expressed in right hemisphere of cerebellum and 202 other cell types or tissues. DR ExpressionAtlas; Q9ULK4; baseline and differential. 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:ComplexPortal. DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI. DR GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc. DR GO; GO:0010628; P:positive regulation of gene expression; IBA:GO_Central. DR GO; GO:2000409; P:positive regulation of T cell extravasation; IEA:Ensembl. DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; NAS:ComplexPortal. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; TAS:ProtInc. DR InterPro; IPR021629; Mediator_Med23. DR PANTHER; PTHR12691; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 23; 1. DR PANTHER; PTHR12691:SF10; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 23; 1. DR Pfam; PF11573; Med23; 1. DR Genevisible; Q9ULK4; HS. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; Direct protein sequencing; KW Disease variant; Intellectual disability; Nucleus; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1..1368 FT /note="Mediator of RNA polymerase II transcription subunit FT 23" FT /id="PRO_0000079358" FT REGION 1343..1368 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1349..1368 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 292 FT /note="Q -> QTLNIAQ (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:11230166, FT ECO:0000303|PubMed:9989412" FT /id="VSP_004034" FT VAR_SEQ 457..475 FT /note="FLQQSLRNKSLQMNDYKIA -> SAFANCFQITCMGDLTHTP (in FT isoform 6)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_047860" FT VAR_SEQ 476..1368 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_047861" FT VAR_SEQ 870..880 FT /note="AMRSHEGNEAQ -> VRINTFLSLFS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9989412" FT /id="VSP_004036" FT VAR_SEQ 881..1368 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9989412" FT /id="VSP_004037" FT VAR_SEQ 1360..1368 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:11230166, FT ECO:0000303|PubMed:15489334" FT /id="VSP_004035" FT VAR_SEQ 1361..1368 FT /note="PVSLPVTQ -> DTLT (in isoform 5)" FT /evidence="ECO:0000303|PubMed:10353252" FT /id="VSP_028380" FT VARIANT 611 FT /note="R -> Q (in MRT18; specifically impairs the response FT of JUN and FOS immediate early genes to serum mitogens by FT altering the interaction between enhancer-bound FT transcription factors TCF7L2 and ELK1 and the Mediator FT complex; dbSNP:rs370667926)" FT /evidence="ECO:0000269|PubMed:21868677" FT /id="VAR_082644" FT CONFLICT 59 FT /note="C -> W (in Ref. 9; AAH60759)" FT /evidence="ECO:0000305" FT CONFLICT 131 FT /note="Y -> N (in Ref. 1; AAD31729)" FT /evidence="ECO:0000305" FT CONFLICT 208 FT /note="F -> V (in Ref. 2; AAD30202)" FT /evidence="ECO:0000305" FT CONFLICT 230 FT /note="V -> E (in Ref. 2; AAD30202)" FT /evidence="ECO:0000305" FT CONFLICT 464 FT /note="N -> H (in Ref. 2; AAD30202)" FT /evidence="ECO:0000305" FT CONFLICT 488 FT /note="F -> V (in Ref. 2; AAD30202)" FT /evidence="ECO:0000305" FT CONFLICT 507 FT /note="I -> L (in Ref. 2; AAD30202)" FT /evidence="ECO:0000305" FT CONFLICT 518 FT /note="G -> A (in Ref. 2; AAD30202)" FT /evidence="ECO:0000305" FT HELIX 2..21 FT /evidence="ECO:0007829|PDB:6H02" FT STRAND 24..26 FT /evidence="ECO:0007829|PDB:6H02" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 35..40 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 42..49 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 56..68 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 73..88 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 94..103 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 112..125 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 126..128 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 131..146 FT /evidence="ECO:0007829|PDB:6H02" FT STRAND 154..156 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 157..160 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 162..170 FT /evidence="ECO:0007829|PDB:6H02" FT TURN 173..176 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 180..190 FT /evidence="ECO:0007829|PDB:6H02" FT TURN 199..202 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 203..210 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 213..218 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 224..226 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 239..241 FT /evidence="ECO:0007829|PDB:6H02" FT TURN 245..247 FT /evidence="ECO:0007829|PDB:6H02" FT STRAND 253..255 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 260..263 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 267..274 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 280..287 FT /evidence="ECO:0007829|PDB:6H02" FT STRAND 291..293 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 298..315 FT /evidence="ECO:0007829|PDB:6H02" FT STRAND 319..324 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 328..343 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 349..360 FT /evidence="ECO:0007829|PDB:6H02" FT TURN 361..363 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 369..383 FT /evidence="ECO:0007829|PDB:6H02" FT TURN 384..386 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 389..391 FT /evidence="ECO:0007829|PDB:6H02" FT TURN 392..394 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 395..402 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 419..422 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 424..437 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 452..462 FT /evidence="ECO:0007829|PDB:6H02" FT STRAND 469..472 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 473..480 FT /evidence="ECO:0007829|PDB:6H02" FT TURN 481..483 FT /evidence="ECO:0007829|PDB:7EMF" FT TURN 485..488 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 489..500 FT /evidence="ECO:0007829|PDB:6H02" FT STRAND 506..508 FT /evidence="ECO:0007829|PDB:6H02" FT STRAND 510..513 FT /evidence="ECO:0007829|PDB:6H02" FT STRAND 515..518 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 525..528 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 533..552 FT /evidence="ECO:0007829|PDB:6H02" FT STRAND 556..558 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 561..570 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 574..576 FT /evidence="ECO:0007829|PDB:6H02" FT TURN 577..580 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 581..586 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 588..594 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 599..611 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 617..632 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 639..654 FT /evidence="ECO:0007829|PDB:6H02" FT TURN 658..660 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 661..665 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 666..668 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 672..675 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 681..697 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 712..720 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 729..732 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 737..744 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 753..767 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 773..780 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 789..799 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 805..814 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 816..835 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 841..855 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 862..870 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 876..891 FT /evidence="ECO:0007829|PDB:6H02" FT STRAND 892..894 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 895..906 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 911..913 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 917..927 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 935..939 FT /evidence="ECO:0007829|PDB:6H02" FT STRAND 940..943 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 959..976 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 978..980 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 981..991 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 992..997 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1001..1011 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1013..1016 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1020..1032 FT /evidence="ECO:0007829|PDB:6H02" FT TURN 1033..1037 FT /evidence="ECO:0007829|PDB:6H02" FT STRAND 1042..1044 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1048..1051 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1065..1080 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1092..1094 FT /evidence="ECO:0007829|PDB:6H02" FT STRAND 1095..1099 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1100..1114 FT /evidence="ECO:0007829|PDB:6H02" FT STRAND 1115..1117 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1119..1131 FT /evidence="ECO:0007829|PDB:6H02" FT STRAND 1135..1137 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1142..1155 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1158..1161 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1163..1172 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1175..1178 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1188..1190 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1193..1197 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 1200..1217 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1221..1224 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1227..1233 FT /evidence="ECO:0007829|PDB:6H02" FT TURN 1234..1238 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1242..1252 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1253..1255 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1256..1262 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1264..1284 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1291..1304 FT /evidence="ECO:0007829|PDB:6H02" FT TURN 1305..1308 FT /evidence="ECO:0007829|PDB:6H02" FT STRAND 1309..1311 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1312..1318 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1323..1328 FT /evidence="ECO:0007829|PDB:6H02" FT HELIX 1329..1331 FT /evidence="ECO:0007829|PDB:6H02" SQ SEQUENCE 1368 AA; 156474 MW; 2BEE9FF5E328477D CRC64; METQLQSIFE EVVKTEVIEE AFPGMFMDTP EDEKTKLISC LGAFRQFWGG LSQESHEQCI QWIVKFIHGQ HSPKRISFLY DCLAMAVETG LLPPRLVCES LINSDTLEWE RTQLWALTFK LVRKIIGGVD YKGVRDLLKV ILEKILTIPN TVSSAVVQQL LAAREVIAYI LERNACLLPA YFAVTEIRKL YPEGKLPHWL LGNLVSDFVD TFRPTARINS ICGRCSLLPV VNNSGAICNS WKLDPATLRF PLKGLLPYDK DLFEPQTALL RYVLEQPYSR DMVCNMLGLN KQHKQRCPVL EDQLVDLVVY AMERSETEEK FDDGGTSQLL WQHLSSQLIF FVLFQFASFP HMVLSLHQKL AGRGLIKGRD HLMWVLLQFI SGSIQKNALA DFLPVMKLFD LLYPEKEYIP VPDINKPQST HAFAMTCIWI HLNRKAQNDN SKLQIPIPHS LRLHHEFLQQ SLRNKSLQMN DYKIALLCNA YSTNSECFTL PMGALVETIY GNGIMRIPLP GTNCMASGSI TPLPMNLLDS LTVHAKMSLI HSIATRVIKL AHAKSSVALA PALVETYSRL LVYMEIESLG IKGFISQLLP TVFKSHAWGI LHTLLEMFSY RMHHIQPHYR VQLLSHLHTL AAVAQTNQNQ LHLCVESTAL RLITALGSSE VQPQFTRFLS DPKTVLSAES EELNRALILT LARATHVTDF FTGSDSIQGT WCKDILQTIM SFTPHNWASH TLSCFPGPLQ AFFKQNNVPQ ESRFNLKKNV EEEYRKWKSM SNENDIITHF SMQGSPPLFL CLLWKMLLET DHINQIGYRV LERIGARALV AHVRTFADFL VYEFSTSAGG QQLNKCIEIL NDMVWKYNIV TLDRLILCLA MRSHEGNEAQ VCYFIIQLLL LKPNDFRNRV SDFVKENSPE HWLQNDWHTK HMNYHKKYPE KLYFEGLAEQ VDPPVQIQSP YLPIYFGNVC LRFLPVFDIV IHRFLELLPV SKSLETLLDH LGGLYKFHDR PVTYLYNTLH YYEMHLRDRA FLKRKLVHAI IGSLKDNRPQ GWCLSDTYLK CAMNAREENP WVPDDTYYCR LIGRLVDTMA GKSPGPFPNC DWRFNEFPNP AAHALHVTCV ELMALAVSGK EVGNALLNVV LKSQPLVPRE NITAWMNAIG LIITALPEPY WIVLHDRIVS VISSPSLTSE TEWVGYPFRL FDFTACHQSY SEMSCSYTLA LAHAVWHHSS IGQLSLIPKF LTEVLLPIVK TEFQLLYVYH LVGPFLQRFQ QERTRCMIEI GVAFYDMLLN VDQCSTHLNY MDPICDFLYH MKYMFTGDSV KEQVEKIICN LKPALKLRLR FITHISKMEP AAVPPQAMNS GSPAPQSNQV PVSLPVTQ //