MED7_HUMAN
ID MED7_HUMAN Reviewed; 233 AA.
AC O43513;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 7;
DE Short=hMED7;
DE AltName: Full=Activator-recruited cofactor 34 kDa component;
DE Short=ARC34;
DE AltName: Full=Cofactor required for Sp1 transcriptional activation subunit 9;
DE Short=CRSP complex subunit 9;
DE AltName: Full=Mediator complex subunit 7;
DE AltName: Full=RNA polymerase transcriptional regulation mediator subunit 7 homolog;
DE AltName: Full=Transcriptional coactivator CRSP33;
GN Name=MED7; Synonyms=ARC34, CRSP9;
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].
RX PubMed=9671713; DOI=10.1073/pnas.95.15.8538;
RA Jiang Y.W., Veschambre P., Erdjument-Bromage H., Tempst P., Conaway J.W.,
RA Conaway R.C., Kornberg R.D.;
RT "Mammalian mediator of transcriptional regulation and its possible role as
RT an end-point of signal transduction pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8538-8543(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Urinary bladder;
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 IN ARC COMPLEX, AND PROTEIN SEQUENCE OF 19-29 AND 212-222.
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 [5]
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 [6]
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 [7]
RP SUMOYLATION.
RX PubMed=17709345; DOI=10.1093/nar/gkm617;
RA Jakobs A., Himstedt F., Funk M., Korn B., Gaestel M., Niedenthal R.;
RT "Ubc9 fusion-directed SUMOylation identifies constitutive and inducible
RT SUMOylation.";
RL Nucleic Acids Res. 35:E109-E109(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-185, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-185, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-185, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-185, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-185, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
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:10235267, ECO:0000269|PubMed:15175163,
CC ECO:0000269|PubMed:15989967}.
CC -!- INTERACTION:
CC O43513; Q9Y376: CAB39; NbExp=3; IntAct=EBI-394632, EBI-306905;
CC O43513; A0A0S2Z4Q4: HGS; NbExp=3; IntAct=EBI-394632, EBI-16429135;
CC O43513; O14964: HGS; NbExp=4; IntAct=EBI-394632, EBI-740220;
CC O43513; Q15648: MED1; NbExp=6; IntAct=EBI-394632, EBI-394459;
CC O43513; Q9BTT4: MED10; NbExp=7; IntAct=EBI-394632, EBI-394354;
CC O43513; Q13503: MED21; NbExp=3; IntAct=EBI-394632, EBI-394678;
CC O43513; O95402: MED26; NbExp=8; IntAct=EBI-394632, EBI-394392;
CC O43513; Q9Y3C7: MED31; NbExp=3; IntAct=EBI-394632, EBI-394707;
CC O43513; P03383: env; Xeno; NbExp=3; IntAct=EBI-394632, EBI-9676086;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Constitutively sumoylated. {ECO:0000269|PubMed:17709345}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 7 family.
CC {ECO:0000305}.
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DR EMBL; AF031383; AAC52115.1; -; mRNA.
DR EMBL; AF104251; AAD12720.1; -; mRNA.
DR EMBL; BC005250; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS4334.1; -.
DR RefSeq; NP_001094286.1; NM_001100816.1.
DR RefSeq; NP_004261.1; NM_004270.4.
DR PDB; 7EMF; EM; 3.50 A; G=1-233.
DR PDB; 7ENA; EM; 4.07 A; g=1-233.
DR PDB; 7ENC; EM; 4.13 A; g=1-233.
DR PDB; 7ENJ; EM; 4.40 A; G=1-233.
DR PDB; 7LBM; EM; 4.80 A; t=1-233.
DR PDB; 7NVR; EM; 4.50 A; i=1-233.
DR PDBsum; 7EMF; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7ENJ; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR AlphaFoldDB; O43513; -.
DR SMR; O43513; -.
DR BioGRID; 114833; 92.
DR ComplexPortal; CPX-3227; Core mediator complex.
DR CORUM; O43513; -.
DR IntAct; O43513; 65.
DR MINT; O43513; -.
DR STRING; 9606.ENSP00000286317; -.
DR iPTMnet; O43513; -.
DR PhosphoSitePlus; O43513; -.
DR BioMuta; MED7; -.
DR EPD; O43513; -.
DR jPOST; O43513; -.
DR MassIVE; O43513; -.
DR PaxDb; O43513; -.
DR PeptideAtlas; O43513; -.
DR PRIDE; O43513; -.
DR ProteomicsDB; 49002; -.
DR Antibodypedia; 16528; 248 antibodies from 25 providers.
DR DNASU; 9443; -.
DR Ensembl; ENST00000286317.6; ENSP00000286317.5; ENSG00000155868.8.
DR Ensembl; ENST00000420343.1; ENSP00000401046.1; ENSG00000155868.8.
DR GeneID; 9443; -.
DR KEGG; hsa:9443; -.
DR MANE-Select; ENST00000286317.6; ENSP00000286317.5; NM_004270.5; NP_004261.1.
DR CTD; 9443; -.
DR DisGeNET; 9443; -.
DR GeneCards; MED7; -.
DR HGNC; HGNC:2378; MED7.
DR HPA; ENSG00000155868; Low tissue specificity.
DR MIM; 605045; gene.
DR neXtProt; NX_O43513; -.
DR OpenTargets; ENSG00000155868; -.
DR PharmGKB; PA162395669; -.
DR VEuPathDB; HostDB:ENSG00000155868; -.
DR eggNOG; KOG0570; Eukaryota.
DR GeneTree; ENSGT00940000154444; -.
DR InParanoid; O43513; -.
DR OMA; PQHFDRR; -.
DR OrthoDB; 1356482at2759; -.
DR PhylomeDB; O43513; -.
DR TreeFam; TF314411; -.
DR PathwayCommons; O43513; -.
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; O43513; -.
DR SIGNOR; O43513; -.
DR BioGRID-ORCS; 9443; 640 hits in 1102 CRISPR screens.
DR ChiTaRS; MED7; human.
DR GeneWiki; MED7; -.
DR GenomeRNAi; 9443; -.
DR Pharos; O43513; Tbio.
DR PRO; PR:O43513; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O43513; protein.
DR Bgee; ENSG00000155868; Expressed in choroid plexus epithelium and 210 other tissues.
DR ExpressionAtlas; O43513; baseline and differential.
DR Genevisible; O43513; HS.
DR GO; GO:0070847; C:core mediator complex; IPI:ComplexPortal.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
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:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
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; IDA:MGI.
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 GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:ProtInc.
DR Gene3D; 6.10.140.200; -; 1.
DR InterPro; IPR037212; Med7/Med21-like.
DR InterPro; IPR009244; Mediatior_Med7.
DR InterPro; IPR044888; Mediatior_Med7_sf.
DR Pfam; PF05983; Med7; 1.
DR SUPFAM; SSF140718; SSF140718; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Direct protein sequencing; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..233
FT /note="Mediator of RNA polymerase II transcription subunit
FT 7"
FT /id="PRO_0000079408"
FT REGION 187..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 74..98
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 104..124
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 126..174
FT /evidence="ECO:0007829|PDB:7EMF"
SQ SEQUENCE 233 AA; 27245 MW; 9D95A2A8360B9C62 CRC64;
MGEPQQVSAL PPPPMQYIKE YTDENIQEGL APKPPPPIKD SYMMFGNQFQ CDDLIIRPLE
SQGIERLHPM QFDHKKELRK LNMSILINFL DLLDILIRSP GSIKREEKLE DLKLLFVHVH
HLINEYRPHQ ARETLRVMME VQKRQRLETA ERFQKHLERV IEMIQNCLAS LPDDLPHSEA
GMRVKTEPMD ADDSNNCTGQ NEHQRENSGH RRDQIIEKDA ALCVLIDEMN ERP
