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Protein

Mediator of RNA polymerase II transcription subunit 7

Gene

MED7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.3 Publications

GO - Molecular functioni

GO - Biological processi

  • negative regulation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-33529-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Mediator of RNA polymerase II transcription subunit 7
Alternative name(s):
Mediator complex subunit 7
Gene namesi
Name:MED7
Ordered Locus Names:YOL135C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL135C.
SGDiS000005495. MED7.

Subcellular locationi

GO - Cellular componenti

  • core mediator complex Source: SGD
  • mediator complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 222222Mediator of RNA polymerase II transcription subunit 7PRO_0000096393Add
BLAST

Proteomic databases

MaxQBiQ08278.
PeptideAtlasiQ08278.

PTM databases

iPTMnetiQ08278.

Interactioni

Subunit structurei

Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. MED7 interacts directly with MED1, MED4 and SRB7/MED21.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CSE2P333083EBI-10674,EBI-5174
MED1Q123214EBI-10674,EBI-32854
MED4Q123435EBI-10674,EBI-31503
NUT2Q062136EBI-10674,EBI-12414
SRB7P478226EBI-10674,EBI-18046

Protein-protein interaction databases

BioGridi34241. 159 interactions.
DIPiDIP-1435N.
IntActiQ08278. 47 interactions.
MINTiMINT-390686.

Structurei

Secondary structure

1
222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 225Combined sources
Helixi25 – 3915Combined sources
Helixi61 – 655Combined sources
Helixi74 – 763Combined sources
Helixi112 – 13322Combined sources
Beta strandi135 – 1373Combined sources
Helixi141 – 1433Combined sources
Helixi144 – 16421Combined sources
Helixi166 – 20338Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YKEX-ray3.30A/C102-205[»]
1YKHX-ray3.00A102-205[»]
3FBIX-ray2.80A/C2-83[»]
3FBNX-ray3.01A/C2-83[»]
ProteinModelPortaliQ08278.
SMRiQ08278. Positions 11-83, 108-205.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08278.

Family & Domainsi

Sequence similaritiesi

Belongs to the Mediator complex subunit 7 family.Curated

Phylogenomic databases

GeneTreeiENSGT00530000064187.
HOGENOMiHOG000000771.
InParanoidiQ08278.
KOiK15148.
OMAiHHILNEY.
OrthoDBiEOG7DJSZ5.

Family and domain databases

InterProiIPR009244. Mediatior_Med7.
[Graphical view]
PANTHERiPTHR21428. PTHR21428. 1 hit.
PfamiPF05983. Med7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q08278-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNDPGNEVS SLYPPPPPYV KFFTQSNLEK LPKYKEKKAA SAKQTAPNNS
60 70 80 90 100
NGGSEEEITC ALDYLIPPPM PKNQQYRAFG SIWQVKDQLP DLESMGLTQL
110 120 130 140 150
YKKSTENEST NYQYKIQELR KLLKSLLLNY LELIGVLSIN PDMYERKVEN
160 170 180 190 200
IRTILVNIHH LLNEYRPHQS RESLIMLLEE QLEYKRGEIR EIEQVCKQVH
210 220
DKLTSIQDTL RTGSQSPPSS SQ
Length:222
Mass (Da):25,585
Last modified:November 1, 1996 - v1
Checksum:iA88301E4EF3223C9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95465 Genomic DNA. Translation: CAA64734.1.
Z74877 Genomic DNA. Translation: CAA99156.1.
AY692889 Genomic DNA. Translation: AAT92908.1.
BK006948 Genomic DNA. Translation: DAA10650.1.
PIRiS66832.
RefSeqiNP_014506.1. NM_001183389.1.

Genome annotation databases

EnsemblFungiiYOL135C; YOL135C; YOL135C.
GeneIDi853985.
KEGGisce:YOL135C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95465 Genomic DNA. Translation: CAA64734.1.
Z74877 Genomic DNA. Translation: CAA99156.1.
AY692889 Genomic DNA. Translation: AAT92908.1.
BK006948 Genomic DNA. Translation: DAA10650.1.
PIRiS66832.
RefSeqiNP_014506.1. NM_001183389.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YKEX-ray3.30A/C102-205[»]
1YKHX-ray3.00A102-205[»]
3FBIX-ray2.80A/C2-83[»]
3FBNX-ray3.01A/C2-83[»]
ProteinModelPortaliQ08278.
SMRiQ08278. Positions 11-83, 108-205.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34241. 159 interactions.
DIPiDIP-1435N.
IntActiQ08278. 47 interactions.
MINTiMINT-390686.

PTM databases

iPTMnetiQ08278.

Proteomic databases

MaxQBiQ08278.
PeptideAtlasiQ08278.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL135C; YOL135C; YOL135C.
GeneIDi853985.
KEGGisce:YOL135C.

Organism-specific databases

EuPathDBiFungiDB:YOL135C.
SGDiS000005495. MED7.

Phylogenomic databases

GeneTreeiENSGT00530000064187.
HOGENOMiHOG000000771.
InParanoidiQ08278.
KOiK15148.
OMAiHHILNEY.
OrthoDBiEOG7DJSZ5.

Enzyme and pathway databases

BioCyciYEAST:G3O-33529-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ08278.
NextBioi975458.
PROiQ08278.

Family and domain databases

InterProiIPR009244. Mediatior_Med7.
[Graphical view]
PANTHERiPTHR21428. PTHR21428. 1 hit.
PfamiPF05983. Med7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of a 12 801 bp fragment of the left arm of yeast chromosome XV containing a putative 6-phosphofructo-2-kinase gene, a gene for a possible glycophospholipid-anchored surface protein and six other open reading frames."
    Aldea M., Piedrafita L., Casas C., Casamayor A., Khalid H., Balcells L., Arino J., Herrero E.
    Yeast 12:1053-1058(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "The Med proteins of yeast and their function through the RNA polymerase II carboxy-terminal domain."
    Myers L.C., Gustafsson C.M., Bushnell D.A., Lui M., Erdjument-Bromage H., Tempst P., Kornberg R.D.
    Genes Dev. 12:45-54(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, COMPONENT OF MEDIATOR COMPLEX.
  6. "The structural and functional organization of the yeast mediator complex."
    Kang J.S., Kim S.H., Hwang M.S., Han S.J., Lee Y.C., Kim Y.-J.
    J. Biol. Chem. 276:42003-42010(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MED1; MED4 AND SRB7, FUNCTION OF THE MEDIATOR COMPLEX, INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Association of the Mediator complex with enhancers of active genes."
    Kuras L., Borggrefe T., Kornberg R.D.
    Proc. Natl. Acad. Sci. U.S.A. 100:13887-13891(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH PROMOTER REGIONS.
  10. Cited for: NOMENCLATURE.
  11. Cited for: STRUCTURE OF THE MEDIATOR COMPLEX.
  12. "Preponderance of free mediator in the yeast Saccharomyces cerevisiae."
    Takagi Y., Chadick J.Z., Davis J.A., Asturias F.J.
    J. Biol. Chem. 280:31200-31207(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE MEDIATOR COMPLEX.
  13. "Mediator and TFIIH govern carboxyl-terminal domain-dependent transcription in yeast extracts."
    Nair D., Kim Y., Myers L.C.
    J. Biol. Chem. 280:33739-33748(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE MEDIATOR COMPLEX.
  14. "Mediator as a general transcription factor."
    Takagi Y., Kornberg R.D.
    J. Biol. Chem. 281:80-89(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE MEDIATOR COMPLEX.
  15. "Genome-wide location of the coactivator mediator: binding without activation and transient Cdk8 interaction on DNA."
    Andrau J.-C., van de Pasch L., Lijnzaad P., Bijma T., Koerkamp M.G., van de Peppel J., Werner M., Holstege F.C.P.
    Mol. Cell 22:179-192(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  16. "Med19(Rox3) regulates intermodule interactions in the Saccharomyces cerevisiae mediator complex."
    Baidoobonso S.M., Guidi B.W., Myers L.C.
    J. Biol. Chem. 282:5551-5559(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE MEDIATOR COMPLEX, INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
  17. "Structure of the yeast RNA polymerase II holoenzyme: mediator conformation and polymerase interaction."
    Davis J.A., Takagi Y., Kornberg R.D., Asturias F.J.
    Mol. Cell 10:409-415(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ELECTRON MICROSCOPY OF MEDIATOR COMPLEX IN COMPLEX WITH RNA POLYMERASE II.
  18. "A conserved mediator hinge revealed in the structure of the MED7-MED21 (Med7-Srb7) heterodimer."
    Baumli S., Hoeppner S., Cramer P.
    J. Biol. Chem. 280:18171-18178(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 102-205 IN COMPLEX WITH SRB7.

Entry informationi

Entry nameiMED7_YEAST
AccessioniPrimary (citable) accession number: Q08278
Secondary accession number(s): D6W1T4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 7598 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.