MED21_HUMAN
ID MED21_HUMAN Reviewed; 144 AA.
AC Q13503; B2R4I3; Q6IB05; Q92811;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 21;
DE AltName: Full=Mediator complex subunit 21;
DE AltName: Full=RNA polymerase II holoenzyme component SRB7;
DE Short=RNAPII complex component SRB7;
DE Short=hSrb7;
GN Name=MED21; Synonyms=SRB7, SURB7;
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], AND INTERACTION WITH RNA POLYMERASE II.
RX PubMed=8598913; DOI=10.1038/380082a0;
RA Chao D.M., Gadbois E.L., Murray P.J., Anderson S.F., Sonu M.S.,
RA Parvin J.D., Young R.A.;
RT "A mammalian SRB protein associated with an RNA polymerase II holoenzyme.";
RL Nature 380:82-85(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH RNA POLYMERASE II.
RC TISSUE=Liver;
RX PubMed=8609996; DOI=10.1038/381086a0;
RA Maldonado E., Shiekhattar R., Sheldon M., Cho H., Drapkin R., Rickert P.,
RA Lees E., Anderson C.W., Linn S., Reinberg D.;
RT "A human RNA polymerase II complex associated with SRB and DNA-repair
RT proteins.";
RL Nature 381:86-89(1996).
RN [3]
RP ERRATUM OF PUBMED:8609996.
RA Maldonado E., Shiekhattar R., Sheldon M., Cho H., Drapkin R., Rickert P.,
RA Lees E., Anderson C.W., Linn S., Reinberg D.;
RL Nature 384:384-384(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
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 [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [8]
RP FUNCTION.
RX PubMed=9660976; DOI=10.1016/s1097-2765(00)80092-1;
RA Oelgeschlaeger T., Tao Y., Kang Y.K., Roeder R.G.;
RT "Transcription activation via enhanced preinitiation complex assembly in a
RT human cell-free system lacking TAFIIs.";
RL Mol. Cell 1:925-931(1998).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A FORM OF THE
RP MEDIATOR COMPLEX.
RX PubMed=9734358; DOI=10.1016/s1097-2765(00)80131-8;
RA Sun X., Zhang Y., Cho H., Rickert P., Lees E., Lane W.S., Reinberg D.;
RT "NAT, a human complex containing Srb polypeptides that functions as a
RT negative regulator of activated transcription.";
RL Mol. Cell 2:213-222(1998).
RN [10]
RP INTERACTION WITH RNA POLYMERASE II AND MED21.
RX PubMed=9933582; DOI=10.1074/jbc.274.7.3937;
RA Xiao H., Tao Y., Roeder R.G.;
RT "The human homologue of Drosophila TRF-proximal protein is associated with
RT an RNA polymerase II-SRB complex.";
RL J. Biol. Chem. 274:3937-3940(1999).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SMCC
RP COMPLEX.
RX PubMed=10024883; DOI=10.1016/s1097-2765(00)80178-1;
RA Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E.,
RA Qin J., Roeder R.G.;
RT "A novel human SRB/MED-containing cofactor complex, SMCC, involved in
RT transcription regulation.";
RL Mol. Cell 3:97-108(1999).
RN [12]
RP ERRATUM OF PUBMED:10024883.
RA Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E.,
RA Qin J., Roeder R.G.;
RL Mol. Cell 3:541-541(1999).
RN [13]
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 [14]
RP FUNCTION, AND INTERACTION WITH THRA.
RX PubMed=15249124; DOI=10.1016/j.mce.2004.05.003;
RA Nevado J., Tenbaum S.P., Aranda A.;
RT "hSrb7, an essential human Mediator component, acts as a coactivator for
RT the thyroid hormone receptor.";
RL Mol. Cell. Endocrinol. 222:41-51(2004).
RN [15]
RP INTERACTION WITH MED1; MED6; MED12; MED13; MED16; MED17; MED18; MED20;
RP MED24; MED28 AND MED30, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION
RP IN THE MEDIATOR COMPLEX, AND ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA
RP 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).
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. {ECO:0000269|PubMed:15249124,
CC ECO:0000269|PubMed:9660976}.
CC -!- SUBUNIT: Interacts with PPARG (By similarity). Component of the
CC Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8,
CC MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17,
CC MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27,
CC MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13,
CC CCNC and CDK8 subunits form a distinct module termed the CDK8 module.
CC Mediator containing the CDK8 module is less active than Mediator
CC lacking this module in supporting transcriptional activation.
CC Individual preparations of the Mediator complex lacking one or more
CC distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC
CC and TRAP. Interacts with THRA in a ligand-dependent fashion.
CC {ECO:0000250, ECO:0000269|PubMed:10024883, ECO:0000269|PubMed:15175163,
CC ECO:0000269|PubMed:15249124, ECO:0000269|PubMed:15989967,
CC ECO:0000269|PubMed:8598913, ECO:0000269|PubMed:8609996,
CC ECO:0000269|PubMed:9734358, ECO:0000269|PubMed:9933582}.
CC -!- INTERACTION:
CC Q13503; Q9UL45: BLOC1S6; NbExp=3; IntAct=EBI-394678, EBI-465781;
CC Q13503; Q96GS4: BORCS6; NbExp=3; IntAct=EBI-394678, EBI-10193358;
CC Q13503; O14964: HGS; NbExp=3; IntAct=EBI-394678, EBI-740220;
CC Q13503; O14901: KLF11; NbExp=3; IntAct=EBI-394678, EBI-948266;
CC Q13503; Q13449: LSAMP; NbExp=3; IntAct=EBI-394678, EBI-4314821;
CC Q13503; O15481: MAGEB4; NbExp=6; IntAct=EBI-394678, EBI-751857;
CC Q13503; Q15648: MED1; NbExp=3; IntAct=EBI-394678, EBI-394459;
CC Q13503; Q9NPJ6: MED4; NbExp=5; IntAct=EBI-394678, EBI-394607;
CC Q13503; O43513: MED7; NbExp=3; IntAct=EBI-394678, EBI-394632;
CC Q13503; Q9NWA0: MED9; NbExp=5; IntAct=EBI-394678, EBI-394653;
CC Q13503; Q9NQG6: MIEF1; NbExp=3; IntAct=EBI-394678, EBI-740987;
CC Q13503; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-394678, EBI-2811583;
CC Q13503; P63208-1: SKP1; NbExp=5; IntAct=EBI-394678, EBI-307497;
CC Q13503; A1L4H1: SSC5D; NbExp=6; IntAct=EBI-394678, EBI-10172867;
CC Q13503; Q6ZMU5: TRIM72; NbExp=3; IntAct=EBI-394678, EBI-2341648;
CC Q13503; Q8N720: ZNF655; NbExp=3; IntAct=EBI-394678, EBI-625509;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 21 family.
CC {ECO:0000305}.
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DR EMBL; U46837; AAA98511.1; -; mRNA.
DR EMBL; U52960; AAB06944.1; -; mRNA.
DR EMBL; CR456999; CAG33280.1; -; mRNA.
DR EMBL; AK311838; BAG34780.1; -; mRNA.
DR EMBL; CH471094; EAW96545.1; -; Genomic_DNA.
DR EMBL; BC008380; AAH08380.1; -; mRNA.
DR CCDS; CCDS8711.1; -.
DR PIR; S68454; S68454.
DR RefSeq; NP_004255.2; NM_004264.4.
DR PDB; 7EMF; EM; 3.50 A; U=1-144.
DR PDB; 7ENA; EM; 4.07 A; u=1-144.
DR PDB; 7ENC; EM; 4.13 A; u=1-144.
DR PDB; 7ENJ; EM; 4.40 A; U=1-144.
DR PDB; 7LBM; EM; 4.80 A; x=1-144.
DR PDB; 7NVR; EM; 4.50 A; n=1-144.
DR PDBsum; 7EMF; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7ENJ; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR AlphaFoldDB; Q13503; -.
DR SMR; Q13503; -.
DR BioGRID; 114807; 146.
DR ComplexPortal; CPX-3227; Core mediator complex.
DR CORUM; Q13503; -.
DR DIP; DIP-31471N; -.
DR IntAct; Q13503; 118.
DR MINT; Q13503; -.
DR STRING; 9606.ENSP00000282892; -.
DR iPTMnet; Q13503; -.
DR PhosphoSitePlus; Q13503; -.
DR BioMuta; MED21; -.
DR DMDM; 7531204; -.
DR EPD; Q13503; -.
DR jPOST; Q13503; -.
DR MassIVE; Q13503; -.
DR MaxQB; Q13503; -.
DR PaxDb; Q13503; -.
DR PeptideAtlas; Q13503; -.
DR PRIDE; Q13503; -.
DR ProteomicsDB; 59498; -.
DR TopDownProteomics; Q13503; -.
DR Antibodypedia; 1803; 169 antibodies from 25 providers.
DR DNASU; 9412; -.
DR Ensembl; ENST00000282892.4; ENSP00000282892.3; ENSG00000152944.9.
DR GeneID; 9412; -.
DR KEGG; hsa:9412; -.
DR MANE-Select; ENST00000282892.4; ENSP00000282892.3; NM_004264.5; NP_004255.2.
DR UCSC; uc001rhp.3; human.
DR CTD; 9412; -.
DR DisGeNET; 9412; -.
DR GeneCards; MED21; -.
DR HGNC; HGNC:11473; MED21.
DR HPA; ENSG00000152944; Low tissue specificity.
DR MIM; 603800; gene.
DR neXtProt; NX_Q13503; -.
DR OpenTargets; ENSG00000152944; -.
DR PharmGKB; PA162395485; -.
DR VEuPathDB; HostDB:ENSG00000152944; -.
DR eggNOG; KOG1510; Eukaryota.
DR GeneTree; ENSGT00390000014557; -.
DR HOGENOM; CLU_126757_0_0_1; -.
DR InParanoid; Q13503; -.
DR OrthoDB; 1583203at2759; -.
DR PhylomeDB; Q13503; -.
DR PathwayCommons; Q13503; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR SignaLink; Q13503; -.
DR SIGNOR; Q13503; -.
DR BioGRID-ORCS; 9412; 638 hits in 1097 CRISPR screens.
DR ChiTaRS; MED21; human.
DR GeneWiki; MED21; -.
DR GenomeRNAi; 9412; -.
DR Pharos; Q13503; Tbio.
DR PRO; PR:Q13503; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q13503; protein.
DR Bgee; ENSG00000152944; Expressed in secondary oocyte and 205 other tissues.
DR ExpressionAtlas; Q13503; baseline and differential.
DR Genevisible; Q13503; 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:0003899; F:DNA-directed 5'-3' RNA polymerase activity; TAS:ProtInc.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0001824; P:blastocyst development; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA: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; 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:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR InterPro; IPR037212; Med7/Med21-like.
DR InterPro; IPR021384; Mediator_Med21.
DR PANTHER; PTHR13381; PTHR13381; 1.
DR Pfam; PF11221; Med21; 1.
DR SUPFAM; SSF140718; SSF140718; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..144
FT /note="Mediator of RNA polymerase II transcription subunit
FT 21"
FT /id="PRO_0000096375"
FT CONFLICT 104
FT /note="L -> V (in Ref. 2; AAB06944)"
FT /evidence="ECO:0000305"
FT HELIX 4..28
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 49..75
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 83..132
FT /evidence="ECO:0007829|PDB:7EMF"
SQ SEQUENCE 144 AA; 15564 MW; F786169620EDC126 CRC64;
MADRLTQLQD AVNSLADQFC NAIGVLQQCG PPASFNNIQT AINKDQPANP TEEYAQLFAA
LIARTAKDID VLIDSLPSEE STAALQAASL YKLEEENHEA ATCLEDVVYR GDMLLEKIQS
ALADIAQSQL KTRSGTHSQS LPDS
