Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mediator of RNA polymerase II transcription subunit 17

Gene

SRB4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 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.5 Publications

GO - Molecular functioni

  • activating transcription factor binding Source: SGD
  • RNA polymerase II core promoter sequence-specific DNA binding Source: SGD
  • RNA polymerase II transcription cofactor activity Source: InterPro
  • transcription factor activity, core RNA polymerase II recruiting Source: SGD

GO - Biological processi

  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • RNA polymerase II transcriptional preinitiation complex assembly Source: GOC
  • transcription initiation from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-30206-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Mediator of RNA polymerase II transcription subunit 17
Alternative name(s):
Mediator complex subunit 17
Suppressor of RNA polymerase B 4
Gene namesi
Name:SRB4
Synonyms:MED17
Ordered Locus Names:YER022W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YER022W.
SGDiS000000824. SRB4.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi353 – 3531G → C in SRB4-1; suppresses the phenotypic defects of an RNA polymerase II CTD truncation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 687687Mediator of RNA polymerase II transcription subunit 17PRO_0000096366Add
BLAST

Proteomic databases

MaxQBiP32569.
PeptideAtlasiP32569.
PRIDEiP32569.

PTM databases

iPTMnetiP32569.

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. The head module may also interact with the TFIIF complex. SRB4/MED17 interacts directly with MED6, MED11, ROX3/MED19, SRB2/MED20 and SRB6/MED22. Interacts directly with the activator GAL4.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MED6P387823EBI-18025,EBI-10667
MED8P383045EBI-18025,EBI-20932
SOH1P386334EBI-18025,EBI-17658
SRB6P325705EBI-18025,EBI-18039

GO - Molecular functioni

  • activating transcription factor binding Source: SGD

Protein-protein interaction databases

BioGridi36756. 100 interactions.
DIPiDIP-152N.
IntActiP32569. 27 interactions.
MINTiMINT-473310.

Structurei

Secondary structure

1
687
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi388 – 3969Combined sources
Beta strandi403 – 4086Combined sources
Helixi425 – 44925Combined sources
Helixi450 – 4556Combined sources
Beta strandi457 – 4615Combined sources
Beta strandi464 – 4685Combined sources
Beta strandi470 – 47910Combined sources
Helixi498 – 52427Combined sources
Turni525 – 5273Combined sources
Helixi535 – 5384Combined sources
Helixi542 – 56524Combined sources
Turni566 – 5694Combined sources
Beta strandi574 – 5796Combined sources
Helixi597 – 6048Combined sources
Helixi607 – 6104Combined sources
Beta strandi614 – 6207Combined sources
Beta strandi630 – 6367Combined sources
Beta strandi640 – 6423Combined sources
Beta strandi644 – 6507Combined sources
Turni654 – 6563Combined sources
Beta strandi660 – 6656Combined sources
Helixi667 – 68014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J1Oelectron microscopy16.00I197-616[»]
I669-687[»]
3RJ1X-ray4.30B/I/P109-616[»]
B/I/P669-687[»]
4GWPX-ray4.20B1-687[»]
4GWQX-ray4.50B1-687[»]
4H62X-ray3.00Q377-687[»]
4V1Oelectron microscopy9.70W2-687[»]
ProteinModelPortaliP32569.
SMRiP32569. Positions 182-687.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Mediator complex subunit 17 family.Curated

Phylogenomic databases

HOGENOMiHOG000113527.
InParanoidiP32569.
KOiK15134.
OMAiVRIFTKI.
OrthoDBiEOG7MPRPT.

Family and domain databases

InterProiIPR019313. Mediator_Med17.
[Graphical view]
PfamiPF10156. Med17. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32569-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTEDPDSNH LSSETGIKLA LDPNLITLAL SSNPNSSLHS PTSDEPVPES
60 70 80 90 100
AGKADTSIRL EGDELENKTK KDNDKNLKFL KNKDSLVSNP HEIYGSMPLE
110 120 130 140 150
QLIPIILRQR GPGFKFVDLN EKELQNEIKQ LGSDSSDGHN SEKKDTDGAD
160 170 180 190 200
ENVQIGEDFM EVDYEDKDNP VDSRNETDHK TNENGETDDN IETVMTQEQF
210 220 230 240 250
VKRRRDMLEH INLAMNESSL ALEFVSLLLS SVKESTGMSS MSPFLRKVVK
260 270 280 290 300
PSSLNSDKIP YVAPTKKEYI ELDILNKGWK LQSLNESKDL LRASFNKLSS
310 320 330 340 350
ILQNEHDYWN KIMQSISNKD VIFKIRDRTS GQKLLAIKYG YEDSGSTYKH
360 370 380 390 400
DRGIANIRNN IESQNLDLIP HSSSVFKGTD FVHSVKKFLR VRIFTKIESE
410 420 430 440 450
DDYILSGESV MDRDSESEEA ETKDIRKQIQ LLKKIIFEKE LMYQIKKECA
460 470 480 490 500
LLISYGVSIE NENKVIIELP NEKFEIELLS LDDDSIVNHE QDLPKINDKR
510 520 530 540 550
ANLMLVMLRL LLVVIFKKTL RSRISSPHGL INLNVDDDIL IIRPILGKVR
560 570 580 590 600
FANYKLLLKK IIKDYVLDIV PGSSITETEV EREQPQENKN IDDENITKLN
610 620 630 640 650
KEIRAFDKLL NIPRRELKIN LPLTEHKSPN LSLMLESPNY CNALIHIKFS
660 670 680
AGTEANAVSF DTTFSDFKEV EDFLHFIVAE YIQQKKV
Length:687
Mass (Da):78,476
Last modified:October 1, 1993 - v1
Checksum:iD25B2993A1BADFD6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti430 – 4312QL → PI in CAA40613 (PubMed:1508147).Curated
Sequence conflicti647 – 6471I → T in AAT93185 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12026 Unassigned DNA. Translation: AAA02632.1.
U18778 Genomic DNA. Translation: AAB64555.1.
AY693166 Genomic DNA. Translation: AAT93185.1.
X57338 Genomic DNA. Translation: CAA40613.1.
BK006939 Genomic DNA. Translation: DAA07675.1.
PIRiA40711.
RefSeqiNP_010939.1. NM_001178913.1.

Genome annotation databases

EnsemblFungiiYER022W; YER022W; YER022W.
GeneIDi856743.
KEGGisce:YER022W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12026 Unassigned DNA. Translation: AAA02632.1.
U18778 Genomic DNA. Translation: AAB64555.1.
AY693166 Genomic DNA. Translation: AAT93185.1.
X57338 Genomic DNA. Translation: CAA40613.1.
BK006939 Genomic DNA. Translation: DAA07675.1.
PIRiA40711.
RefSeqiNP_010939.1. NM_001178913.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J1Oelectron microscopy16.00I197-616[»]
I669-687[»]
3RJ1X-ray4.30B/I/P109-616[»]
B/I/P669-687[»]
4GWPX-ray4.20B1-687[»]
4GWQX-ray4.50B1-687[»]
4H62X-ray3.00Q377-687[»]
4V1Oelectron microscopy9.70W2-687[»]
ProteinModelPortaliP32569.
SMRiP32569. Positions 182-687.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36756. 100 interactions.
DIPiDIP-152N.
IntActiP32569. 27 interactions.
MINTiMINT-473310.

PTM databases

iPTMnetiP32569.

Proteomic databases

MaxQBiP32569.
PeptideAtlasiP32569.
PRIDEiP32569.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER022W; YER022W; YER022W.
GeneIDi856743.
KEGGisce:YER022W.

Organism-specific databases

EuPathDBiFungiDB:YER022W.
SGDiS000000824. SRB4.

Phylogenomic databases

HOGENOMiHOG000113527.
InParanoidiP32569.
KOiK15134.
OMAiVRIFTKI.
OrthoDBiEOG7MPRPT.

Enzyme and pathway databases

BioCyciYEAST:G3O-30206-MONOMER.

Miscellaneous databases

NextBioi982879.
PROiP32569.

Family and domain databases

InterProiIPR019313. Mediator_Med17.
[Graphical view]
PfamiPF10156. Med17. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A multisubunit complex associated with the RNA polymerase II CTD and TATA-binding protein in yeast."
    Thompson C.M., Koleske A.J., Chao D.M., Young R.A.
    Cell 73:1361-1375(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-353.
    Strain: Z28.
  2. 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. "ore2, a mutation affecting proline biosynthesis in the yeast Saccharomyces cerevisiae, leads to a cdc phenotype."
    Neuville P., Aigle M.
    Mol. Gen. Genet. 234:193-200(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 430-687.
    Strain: ATCC 44827 / SKQ2N.
  6. "A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA polymerase II."
    Kim Y.-J., Bjoerklund S., Li Y., Sayre M.H., Kornberg R.D.
    Cell 77:599-608(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPONENT OF MEDIATOR COMPLEX.
  7. Cited for: FUNCTION.
  8. "An activator target in the RNA polymerase II holoenzyme."
    Koh S.S., Ansari A.Z., Ptashne M., Young R.A.
    Mol. Cell 1:895-904(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GAL4; SRB2 AND SRB6.
  9. "Interplay of positive and negative regulators in transcription initiation by RNA polymerase II holoenzyme."
    Lee T.I., Wyrick J.J., Koh S.S., Jennings E.G., Gadbois E.L., Young R.A.
    Mol. Cell. Biol. 18:4455-4462(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MED6 AND SRB6.
  10. "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 MED11 AND ROX3, FUNCTION OF THE MEDIATOR COMPLEX, INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. Cited for: NOMENCLATURE.
  14. Cited for: TOPOLOGY OF THE MEDIATOR COMPLEX.
  15. "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: INTERACTION WITH MED6.
  16. "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.
  17. "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.
  18. "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.
  19. "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.
  20. "Activator-specific recruitment of Mediator in vivo."
    Fan X., Chou D.M., Struhl K.
    Nat. Struct. Mol. Biol. 13:117-120(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH PROMOTER REGIONS.
  21. "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.
  22. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "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.
  25. Cited for: ELECTRON MICROSCOPY OF THE MEDIATOR COMPLEX HEAD MODULE, FUNCTION OF THE MEDIATOR COMPLEX HEAD MODULE, INTERACTION OF THE MEDIATOR COMPLEX HEAD MODULE WITH RNA POLYMERASE II AND TFIIF, INTERACTION WITH MED6; MED8; MED11; SRB2; SRB5 AND SRB6.

Entry informationi

Entry nameiMED17_YEAST
AccessioniPrimary (citable) accession number: P32569
Secondary accession number(s): D3DLS1, Q06790, Q6B1B4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: May 11, 2016
This is version 135 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 1720 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 V
    Yeast (Saccharomyces cerevisiae) chromosome V: 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.