MED9_HUMAN
ID MED9_HUMAN Reviewed; 146 AA.
AC Q9NWA0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 9;
DE AltName: Full=Mediator complex subunit 9;
GN Name=MED9; Synonyms=MED25;
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 [LARGE SCALE MRNA].
RC TISSUE=Embryo;
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 [2]
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 (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
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 [5]
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 Q9NWA0; Q13503: MED21; NbExp=5; IntAct=EBI-394653, EBI-394678;
CC Q9NWA0; Q9NPJ6: MED4; NbExp=12; IntAct=EBI-394653, EBI-394607;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 9 family.
CC {ECO:0000305}.
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DR EMBL; AK001055; BAA91483.1; -; mRNA.
DR EMBL; CH471196; EAW55706.1; -; Genomic_DNA.
DR EMBL; BC104988; AAI04989.1; -; mRNA.
DR EMBL; BC112029; AAI12030.1; -; mRNA.
DR CCDS; CCDS11184.1; -.
DR RefSeq; NP_060489.1; NM_018019.2.
DR PDB; 7EMF; EM; 3.50 A; I=1-146.
DR PDB; 7ENA; EM; 4.07 A; i=1-146.
DR PDB; 7ENC; EM; 4.13 A; i=1-146.
DR PDB; 7ENJ; EM; 4.40 A; I=1-146.
DR PDB; 7LBM; EM; 4.80 A; u=1-146.
DR PDB; 7NVR; EM; 4.50 A; j=1-146.
DR PDBsum; 7EMF; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7ENJ; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR AlphaFoldDB; Q9NWA0; -.
DR SMR; Q9NWA0; -.
DR BioGRID; 120403; 95.
DR ComplexPortal; CPX-3227; Core mediator complex.
DR CORUM; Q9NWA0; -.
DR IntAct; Q9NWA0; 78.
DR MINT; Q9NWA0; -.
DR STRING; 9606.ENSP00000268711; -.
DR GlyGen; Q9NWA0; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9NWA0; -.
DR PhosphoSitePlus; Q9NWA0; -.
DR BioMuta; MED9; -.
DR DMDM; 74734632; -.
DR EPD; Q9NWA0; -.
DR jPOST; Q9NWA0; -.
DR MassIVE; Q9NWA0; -.
DR MaxQB; Q9NWA0; -.
DR PaxDb; Q9NWA0; -.
DR PeptideAtlas; Q9NWA0; -.
DR PRIDE; Q9NWA0; -.
DR ProteomicsDB; 82916; -.
DR Antibodypedia; 25454; 145 antibodies from 23 providers.
DR DNASU; 55090; -.
DR Ensembl; ENST00000268711.4; ENSP00000268711.3; ENSG00000141026.6.
DR GeneID; 55090; -.
DR KEGG; hsa:55090; -.
DR MANE-Select; ENST00000268711.4; ENSP00000268711.3; NM_018019.3; NP_060489.1.
DR UCSC; uc002grh.2; human.
DR CTD; 55090; -.
DR DisGeNET; 55090; -.
DR GeneCards; MED9; -.
DR HGNC; HGNC:25487; MED9.
DR HPA; ENSG00000141026; Low tissue specificity.
DR MIM; 609878; gene.
DR neXtProt; NX_Q9NWA0; -.
DR OpenTargets; ENSG00000141026; -.
DR PharmGKB; PA134925396; -.
DR VEuPathDB; HostDB:ENSG00000141026; -.
DR eggNOG; ENOG502S51J; Eukaryota.
DR GeneTree; ENSGT00390000017379; -.
DR HOGENOM; CLU_148111_0_0_1; -.
DR InParanoid; Q9NWA0; -.
DR OMA; TMPGIQL; -.
DR OrthoDB; 1524234at2759; -.
DR PhylomeDB; Q9NWA0; -.
DR TreeFam; TF324926; -.
DR PathwayCommons; Q9NWA0; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR SignaLink; Q9NWA0; -.
DR SIGNOR; Q9NWA0; -.
DR BioGRID-ORCS; 55090; 618 hits in 1090 CRISPR screens.
DR ChiTaRS; MED9; human.
DR GenomeRNAi; 55090; -.
DR Pharos; Q9NWA0; Tbio.
DR PRO; PR:Q9NWA0; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9NWA0; protein.
DR Bgee; ENSG00000141026; Expressed in apex of heart and 120 other tissues.
DR ExpressionAtlas; Q9NWA0; baseline and differential.
DR Genevisible; Q9NWA0; HS.
DR GO; GO:0070847; C:core mediator complex; IPI:ComplexPortal.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
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:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR InterPro; IPR037212; Med7/Med21-like.
DR InterPro; IPR011425; Med9.
DR InterPro; IPR039242; MED9_metazoa.
DR PANTHER; PTHR20844; PTHR20844; 1.
DR Pfam; PF07544; Med9; 1.
DR SUPFAM; SSF140718; SSF140718; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Coiled coil; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..146
FT /note="Mediator of RNA polymerase II transcription subunit
FT 9"
FT /id="PRO_0000304147"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 112..139
FT /evidence="ECO:0000255"
FT COMPBIAS 22..50
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 87..101
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 111..137
FT /evidence="ECO:0007829|PDB:7EMF"
SQ SEQUENCE 146 AA; 16403 MW; 24CDB7CBDFD36D1A CRC64;
MASAGVAAGR QAEDVLPPTS DQPLPDTKPL PPPQPPPVPA PQPQQSPAPR PQSPARAREE
ENYSFLPLVH NIIKCMDKDS PEVHQDLNAL KSKFQEMRKL ISTMPGIHLS PEQQQQQLQS
LREQVRTKNE LLQKYKSLCM FEIPKE
