MED18_HUMAN
ID MED18_HUMAN Reviewed; 208 AA.
AC Q9BUE0; D3DPM1; Q9NXU9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 18;
DE AltName: Full=Mediator complex subunit 18;
DE AltName: Full=p28b;
GN Name=MED18;
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].
RC TISSUE=Lymphoma;
RA Furumoto T., Malik S., Hayashi K., Tanaka A., Ito M., Roeder R.G.,
RA Hanaoka F., Ohkuma Y.;
RT "Physical and functional connections between human Mediator complex and
RT general transcription machinery.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 INTERACTION WITH MED10 AND MED20.
RX PubMed=12584197; DOI=10.1074/jbc.c300054200;
RA Sato S., Tomomori-Sato C., Banks C.A.S., Sorokina I., Parmely T.J.,
RA Kong S.E., Jin J., Cai Y., Lane W.S., Brower C.S., Conaway R.C.,
RA Conaway J.W.;
RT "Identification of mammalian Mediator subunits with similarities to yeast
RT Mediator subunits Srb5, Srb6, Med11, and Rox3.";
RL J. Biol. Chem. 278:15123-15127(2003).
RN [7]
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 [8]
RP INTERACTION WITH CCNC; MED1; MED12; MED13; MED17; MED20 AND MED21,
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR
RP COMPLEX, AND ASSOCIATION 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY
RP 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 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.
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.
CC {ECO:0000269|PubMed:15175163, ECO:0000269|PubMed:15989967}.
CC -!- INTERACTION:
CC Q9BUE0; Q63HM1: AFMID; NbExp=3; IntAct=EBI-394640, EBI-13286382;
CC Q9BUE0; Q13554: CAMK2B; NbExp=3; IntAct=EBI-394640, EBI-1058722;
CC Q9BUE0; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-394640, EBI-10172004;
CC Q9BUE0; Q9NVC6: MED17; NbExp=3; IntAct=EBI-394640, EBI-394562;
CC Q9BUE0; Q9H944: MED20; NbExp=21; IntAct=EBI-394640, EBI-394644;
CC Q9BUE0; Q15528: MED22; NbExp=3; IntAct=EBI-394640, EBI-394687;
CC Q9BUE0; Q9NX70: MED29; NbExp=6; IntAct=EBI-394640, EBI-394656;
CC Q9BUE0; O75586: MED6; NbExp=3; IntAct=EBI-394640, EBI-394624;
CC Q9BUE0; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-394640, EBI-11139477;
CC Q9BUE0; Q9HCM9: TRIM39; NbExp=3; IntAct=EBI-394640, EBI-739510;
CC Q9BUE0; Q9HCM9-2: TRIM39; NbExp=3; IntAct=EBI-394640, EBI-11523450;
CC Q9BUE0; Q9R0X0: Med20; Xeno; NbExp=6; IntAct=EBI-394640, EBI-398698;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 18 family.
CC {ECO:0000305}.
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DR EMBL; AB107222; BAD06869.1; -; mRNA.
DR EMBL; AK000052; BAA90910.1; -; mRNA.
DR EMBL; AL353622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07699.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07700.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07702.1; -; Genomic_DNA.
DR EMBL; BC002694; AAH02694.1; -; mRNA.
DR CCDS; CCDS322.1; -.
DR RefSeq; NP_001120822.1; NM_001127350.1.
DR RefSeq; NP_060108.2; NM_017638.2.
DR RefSeq; XP_005245971.1; XM_005245914.4.
DR PDB; 7EMF; EM; 3.50 A; R=1-208.
DR PDB; 7ENA; EM; 4.07 A; r=1-208.
DR PDB; 7ENC; EM; 4.13 A; r=1-208.
DR PDB; 7ENJ; EM; 4.40 A; R=1-208.
DR PDB; 7LBM; EM; 4.80 A; k=1-208.
DR PDB; 7NVR; EM; 4.50 A; e=1-208.
DR PDBsum; 7EMF; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7ENJ; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR AlphaFoldDB; Q9BUE0; -.
DR SMR; Q9BUE0; -.
DR BioGRID; 120156; 66.
DR ComplexPortal; CPX-3227; Core mediator complex.
DR CORUM; Q9BUE0; -.
DR IntAct; Q9BUE0; 65.
DR MINT; Q9BUE0; -.
DR STRING; 9606.ENSP00000362948; -.
DR iPTMnet; Q9BUE0; -.
DR MetOSite; Q9BUE0; -.
DR PhosphoSitePlus; Q9BUE0; -.
DR BioMuta; MED18; -.
DR DMDM; 74752353; -.
DR EPD; Q9BUE0; -.
DR jPOST; Q9BUE0; -.
DR MassIVE; Q9BUE0; -.
DR MaxQB; Q9BUE0; -.
DR PaxDb; Q9BUE0; -.
DR PeptideAtlas; Q9BUE0; -.
DR PRIDE; Q9BUE0; -.
DR ProteomicsDB; 79079; -.
DR Antibodypedia; 30928; 235 antibodies from 25 providers.
DR DNASU; 54797; -.
DR Ensembl; ENST00000373842.9; ENSP00000362948.4; ENSG00000130772.14.
DR Ensembl; ENST00000398997.2; ENSP00000381963.2; ENSG00000130772.14.
DR Ensembl; ENST00000645794.2; ENSP00000494184.1; ENSG00000284944.2.
DR Ensembl; ENST00000647352.1; ENSP00000494048.1; ENSG00000284944.2.
DR GeneID; 54797; -.
DR KEGG; hsa:54797; -.
DR MANE-Select; ENST00000373842.9; ENSP00000362948.4; NM_017638.3; NP_060108.2.
DR UCSC; uc001bpt.5; human.
DR CTD; 54797; -.
DR DisGeNET; 54797; -.
DR GeneCards; MED18; -.
DR HGNC; HGNC:25944; MED18.
DR HPA; ENSG00000130772; Low tissue specificity.
DR MIM; 612384; gene.
DR neXtProt; NX_Q9BUE0; -.
DR OpenTargets; ENSG00000130772; -.
DR PharmGKB; PA134884523; -.
DR VEuPathDB; HostDB:ENSG00000130772; -.
DR eggNOG; KOG3264; Eukaryota.
DR GeneTree; ENSGT00390000003312; -.
DR HOGENOM; CLU_084570_0_0_1; -.
DR InParanoid; Q9BUE0; -.
DR OMA; PTSPWHL; -.
DR OrthoDB; 1140930at2759; -.
DR PhylomeDB; Q9BUE0; -.
DR TreeFam; TF313246; -.
DR PathwayCommons; Q9BUE0; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR SignaLink; Q9BUE0; -.
DR SIGNOR; Q9BUE0; -.
DR BioGRID-ORCS; 54797; 632 hits in 1095 CRISPR screens.
DR GenomeRNAi; 54797; -.
DR Pharos; Q9BUE0; Tbio.
DR PRO; PR:Q9BUE0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BUE0; protein.
DR Bgee; ENSG00000130772; Expressed in mucosa of transverse colon and 107 other tissues.
DR Genevisible; Q9BUE0; HS.
DR GO; GO:0070847; C:core mediator complex; IPI:ComplexPortal.
DR GO; GO:0016592; C:mediator complex; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
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; IC:ComplexPortal.
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; IC:ComplexPortal.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IBA:GO_Central.
DR InterPro; IPR019095; Mediator_Med18.
DR PANTHER; PTHR13321; PTHR13321; 1.
DR Pfam; PF09637; Med18; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..208
FT /note="Mediator of RNA polymerase II transcription subunit
FT 18"
FT /id="PRO_0000304742"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 148
FT /note="I -> T (in Ref. 2; BAA90910)"
FT /evidence="ECO:0000305"
FT STRAND 18..27
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 29..42
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 51..60
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 68..78
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 94..110
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 124..138
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 141..151
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 165..178
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 192..196
FT /evidence="ECO:0007829|PDB:7EMF"
SQ SEQUENCE 208 AA; 23663 MW; AE68984390532C33 CRC64;
MEAPPVTMMP VTGGTINMME YLLQGSVLDH SLESLIHRLR GLCDNMEPET FLDHEMVFLL
KGQQASPFVL RARRSMDRAG APWHLRYLGQ PEMGDKNRHA LVRNCVDIAT SENLTDFLME
MGFRMDHEFV AKGHLFRKGI MKIMVYKIFR ILVPGNTDST EALSLSYLVE LSVVAPAGQD
MVSDDMKNFA EQLKPLVHLE KIDPKRLM
