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Protein

Mediator of RNA polymerase II transcription subunit 20

Gene

SRB2

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.4 Publications

GO - Molecular functioni

  • protein domain specific binding Source: SGD
  • RNA polymerase II transcription coactivator activity involved in preinitiation complex assembly Source: SGD
  • RNA polymerase II transcription factor activity, TBP-class protein binding, involved in preinitiation complex assembly Source: SGD
  • transcription factor activity, core RNA polymerase II binding Source: SGD
  • transcription factor activity, RNA polymerase II transcription factor recruiting Source: SGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-31100-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Mediator of RNA polymerase II transcription subunit 20
Alternative name(s):
Hyper-recombination suppressor protein 2
Mediator complex subunit 20
Suppressor of RNA polymerase B 2
Gene namesi
Name:SRB2
Synonyms:HRS2, MED20
Ordered Locus Names:YHR041C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR041C.
SGDiS000001083. SRB2.

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
Mutagenesisi14 – 141P → H in SRB2-1; suppresses the phenotypic defects of an RNA polymerase II CTD truncation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 210210Mediator of RNA polymerase II transcription subunit 20PRO_0000096374Add
BLAST

Proteomic databases

MaxQBiP34162.

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. MED1 interacts directly with MED4 and MED7. SRB2/MED20 interacts directly with SRB4/MED17 and SRB5/MED18.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SRB5P325853EBI-18018,EBI-18032

GO - Molecular functioni

  • protein domain specific binding Source: SGD

Protein-protein interaction databases

BioGridi36473. 303 interactions.
DIPiDIP-107N.
IntActiP34162. 20 interactions.
MINTiMINT-473266.

Structurei

Secondary structure

1
210
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Helixi16 – 249Combined sources
Helixi25 – 273Combined sources
Beta strandi30 – 323Combined sources
Beta strandi35 – 4410Combined sources
Beta strandi51 – 533Combined sources
Beta strandi56 – 7318Combined sources
Beta strandi76 – 816Combined sources
Helixi84 – 863Combined sources
Helixi89 – 935Combined sources
Helixi104 – 1118Combined sources
Turni113 – 1153Combined sources
Beta strandi116 – 13217Combined sources
Beta strandi135 – 14410Combined sources
Beta strandi147 – 15812Combined sources
Helixi160 – 1623Combined sources
Helixi163 – 17614Combined sources
Beta strandi183 – 1853Combined sources
Helixi196 – 20813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HZMX-ray2.40A/C/E/G1-210[»]
2HZSX-ray2.70A/C/E/G2-210[»]
3J1Oelectron microscopy16.00M1-210[»]
3RJ1X-ray4.30F/M/T1-210[»]
4GWPX-ray4.20F1-210[»]
4GWQX-ray4.50F1-210[»]
4V1Oelectron microscopy9.70Y2-210[»]
ProteinModelPortaliP34162.
SMRiP34162. Positions 2-210.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP34162.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 210210Ser/Thr/Tyr-richAdd
BLAST

Sequence similaritiesi

Belongs to the Mediator complex subunit 20 family.Curated

Phylogenomic databases

HOGENOMiHOG000113535.
InParanoidiP34162.
OMAiFKIFRNN.
OrthoDBiEOG092C56VU.

Family and domain databases

InterProiIPR016532. Med20.
IPR013921. Mediator_Med20.
[Graphical view]
PfamiPF08612. Med20. 1 hit.
[Graphical view]
PIRSFiPIRSF007945. SRB2. 1 hit.

Sequencei

Sequence statusi: Complete.

P34162-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKSAVIFVE RATPATLTEL KDALSNSILS VRDPWSIDFR TYRCSIKNLP
60 70 80 90 100
ADVSKLMYSI TFHHHGRQTV LIKDNSAMVT TAAAADIPPA LVFNGSSTGV
110 120 130 140 150
PESIDTILSS KLSNIWMQRQ LIKGDAGETL ILDGLTVRLV NLFSSTGFKG
160 170 180 190 200
LLIELQADEA GEFETKIAGI EGHLAEIRAK EYKTSSDSLG PDTSNEICDL
210
AYQYVRALEL
Length:210
Mass (Da):22,894
Last modified:February 1, 1994 - v1
Checksum:iC30BF309D43AFB2A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S36754 Genomic DNA. Translation: AAB22223.1.
U00062 Genomic DNA. Translation: AAB68920.1.
BK006934 Genomic DNA. Translation: DAA06733.1.
PIRiA38105.
RefSeqiNP_011907.1. NM_001179171.1.

Genome annotation databases

EnsemblFungiiYHR041C; YHR041C; YHR041C.
GeneIDi856437.
KEGGisce:YHR041C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S36754 Genomic DNA. Translation: AAB22223.1.
U00062 Genomic DNA. Translation: AAB68920.1.
BK006934 Genomic DNA. Translation: DAA06733.1.
PIRiA38105.
RefSeqiNP_011907.1. NM_001179171.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HZMX-ray2.40A/C/E/G1-210[»]
2HZSX-ray2.70A/C/E/G2-210[»]
3J1Oelectron microscopy16.00M1-210[»]
3RJ1X-ray4.30F/M/T1-210[»]
4GWPX-ray4.20F1-210[»]
4GWQX-ray4.50F1-210[»]
4V1Oelectron microscopy9.70Y2-210[»]
ProteinModelPortaliP34162.
SMRiP34162. Positions 2-210.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36473. 303 interactions.
DIPiDIP-107N.
IntActiP34162. 20 interactions.
MINTiMINT-473266.

Proteomic databases

MaxQBiP34162.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR041C; YHR041C; YHR041C.
GeneIDi856437.
KEGGisce:YHR041C.

Organism-specific databases

EuPathDBiFungiDB:YHR041C.
SGDiS000001083. SRB2.

Phylogenomic databases

HOGENOMiHOG000113535.
InParanoidiP34162.
OMAiFKIFRNN.
OrthoDBiEOG092C56VU.

Enzyme and pathway databases

BioCyciYEAST:G3O-31100-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP34162.
PROiP34162.

Family and domain databases

InterProiIPR016532. Med20.
IPR013921. Mediator_Med20.
[Graphical view]
PfamiPF08612. Med20. 1 hit.
[Graphical view]
PIRSFiPIRSF007945. SRB2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMED20_YEAST
AccessioniPrimary (citable) accession number: P34162
Secondary accession number(s): D3DKY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: September 7, 2016
This is version 137 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 VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: 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.