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Entry version 206 (22 Apr 2020)
Sequence version 1 (01 Feb 1991)
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Protein

DNA-directed RNA polymerases I, II, and III subunit RPABC1

Gene

RPB5

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. RNA polymerase complexes are composed of mobile elements that move relative to each other. In Pol II, RPB5 is part of the lower jaw surrounding the central large cleft and thought to grab the incoming DNA template. Seems to be the major component in this process.3 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding
Biological processRibosome biogenesis, Transcription

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
YEAST:G3O-29104-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-113418 Formation of the Early Elongation Complex
R-SCE-674695 RNA Polymerase II Pre-transcription Events
R-SCE-6781823 Formation of TC-NER Pre-Incision Complex
R-SCE-6782135 Dual incision in TC-NER
R-SCE-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-SCE-6796648 TP53 Regulates Transcription of DNA Repair Genes
R-SCE-6807505 RNA polymerase II transcribes snRNA genes
R-SCE-72086 mRNA Capping
R-SCE-73762 RNA Polymerase I Transcription Initiation
R-SCE-73772 RNA Polymerase I Promoter Escape
R-SCE-73776 RNA Polymerase II Promoter Escape
R-SCE-73779 RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
R-SCE-75953 RNA Polymerase II Transcription Initiation
R-SCE-75955 RNA Polymerase II Transcription Elongation
R-SCE-76042 RNA Polymerase II Transcription Initiation And Promoter Clearance
R-SCE-76061 RNA Polymerase III Transcription Initiation From Type 1 Promoter
R-SCE-76066 RNA Polymerase III Transcription Initiation From Type 2 Promoter
R-SCE-77075 RNA Pol II CTD phosphorylation and interaction with CE
R-SCE-9018519 Estrogen-dependent gene expression

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA-directed RNA polymerases I, II, and III subunit RPABC1
Short name:
RNA polymerases I, II, and III subunit ABC1
Alternative name(s):
ABC27
DNA-directed RNA polymerases I, II, and III 27 kDa polypeptide
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RPB5
Synonyms:RPA7, RPC9
Ordered Locus Names:YBR154C
ORF Names:YBR1204
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome II

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YBR154C

Saccharomyces Genome Database

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SGDi
S000000358 RPB5

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001460861 – 215DNA-directed RNA polymerases I, II, and III subunit RPABC1Add BLAST215

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P20434

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P20434

PRoteomics IDEntifications database

More...
PRIDEi
P20434

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P20434

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the RNA polymerase I (Pol I), RNA polymerase II (Pol II) and RNA polymerase III (Pol III) complexes.

Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that mediates interactions with transcription initiation factors and newly synthesized RNA.

Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits: RPO21, RPB2, RPB3, RPB4, RPB5, RPO26, RPB7, RPB8, RPB9, RPB10 and RPC10.

Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits.

9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Show more details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
32853, 276 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1664 DNA-directed RNA Polymerase I complex
CPX-2660 DNA-directed RNA polymerase III complex
CPX-2662 DNA-directed RNA polymerase II complex

Database of interacting proteins

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DIPi
DIP-71N

Protein interaction database and analysis system

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IntActi
P20434, 56 interactors

Molecular INTeraction database

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MINTi
P20434

STRING: functional protein association networks

More...
STRINGi
4932.YBR154C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P20434 protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1215
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P20434

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P20434

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_058320_0_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P20434

KEGG Orthology (KO)

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KOi
K03013

Identification of Orthologs from Complete Genome Data

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OMAi
MQMCHDR

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.1340.10, 1 hit
3.90.940.20, 1 hit

HAMAP database of protein families

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HAMAPi
MF_00025 RNApol_RpoH_RPB5, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR014381 DNA_RNA_pol_RPB5_euk/virus
IPR005571 RNA_pol_Rpb5_N
IPR036710 RNA_pol_Rpb5_N_sf
IPR000783 RNA_pol_subH/Rpb5_C
IPR020608 RNA_pol_subH/Rpb5_CS
IPR039531 Rpb5-like
IPR035913 RPB5-like_sf
IPR020609 RpoH/RPB5

The PANTHER Classification System

More...
PANTHERi
PTHR10535 PTHR10535, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF01191 RNA_pol_Rpb5_C, 1 hit
PF03871 RNA_pol_Rpb5_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000747 RPB5, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF53036 SSF53036, 1 hit
SSF55287 SSF55287, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS01110 RNA_POL_H_23KD, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P20434-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDQENERNIS RLWRAFRTVK EMVKDRGYFI TQEEVELPLE DFKAKYCDSM
60 70 80 90 100
GRPQRKMMSF QANPTEESIS KFPDMGSLWV EFCDEPSVGV KTMKTFVIHI
110 120 130 140 150
QEKNFQTGIF VYQNNITPSA MKLVPSIPPA TIETFNEAAL VVNITHHELV
160 170 180 190 200
PKHIRLSSDE KRELLKRYRL KESQLPRIQR ADPVALYLGL KRGEVVKIIR
210
KSETSGRYAS YRICM
Length:215
Mass (Da):25,079
Last modified:February 1, 1991 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2A15F7114D69D829
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti37L → W in AAC60556 (PubMed:8488729).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X53287 Genomic DNA Translation: CAA37381.1
X71329 Genomic DNA Translation: CAA50472.1
S59774 Genomic DNA Translation: AAC60556.1
Z36023 Genomic DNA Translation: CAA85113.1
BK006936 Genomic DNA Translation: DAA07269.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A34588

NCBI Reference Sequences

More...
RefSeqi
NP_009712.1, NM_001178502.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YBR154C_mRNA; YBR154C; YBR154C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
852451

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YBR154C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53287 Genomic DNA Translation: CAA37381.1
X71329 Genomic DNA Translation: CAA50472.1
S59774 Genomic DNA Translation: AAC60556.1
Z36023 Genomic DNA Translation: CAA85113.1
BK006936 Genomic DNA Translation: DAA07269.1
PIRiA34588
RefSeqiNP_009712.1, NM_001178502.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DZFX-ray1.90A1-215[»]
1I3QX-ray3.10E1-215[»]
1I50X-ray2.80E1-215[»]
1I6HX-ray3.30E1-215[»]
1K83X-ray2.80E1-215[»]
1NIKX-ray4.10E1-215[»]
1NT9X-ray4.20E1-215[»]
1PQVX-ray3.80E1-215[»]
1R5UX-ray4.50E1-215[»]
1R9SX-ray4.25E1-215[»]
1R9TX-ray3.50E1-215[»]
1SFOX-ray3.61E1-215[»]
1TWAX-ray3.20E1-215[»]
1TWCX-ray3.00E1-215[»]
1TWFX-ray2.30E1-215[»]
1TWGX-ray3.30E1-215[»]
1TWHX-ray3.40E1-215[»]
1WCMX-ray3.80E1-215[»]
1Y1VX-ray3.80E1-215[»]
1Y1WX-ray4.00E1-215[»]
1Y1YX-ray4.00E1-215[»]
1Y77X-ray4.50E1-215[»]
2B63X-ray3.80E1-215[»]
2B8KX-ray4.15E1-215[»]
2E2HX-ray3.95E1-215[»]
2E2IX-ray3.41E1-215[»]
2E2JX-ray3.50E1-215[»]
2JA5X-ray3.80E1-215[»]
2JA6X-ray4.00E1-215[»]
2JA7X-ray3.80E/Q1-215[»]
2JA8X-ray3.80E1-215[»]
2NVQX-ray2.90E1-215[»]
2NVTX-ray3.36E1-215[»]
2NVXX-ray3.60E1-215[»]
2NVYX-ray3.40E1-215[»]
2NVZX-ray4.30E1-215[»]
2R7ZX-ray3.80E1-215[»]
2R92X-ray3.80E1-215[»]
2R93X-ray4.00E1-215[»]
2VUMX-ray3.40E1-215[»]
2YU9X-ray3.40E1-215[»]
3CQZX-ray2.80E1-215[»]
3FKIX-ray3.88E1-215[»]
3GTGX-ray3.78E1-215[»]
3GTJX-ray3.42E1-215[»]
3GTKX-ray3.80E1-215[»]
3GTLX-ray3.38E1-215[»]
3GTMX-ray3.80E1-215[»]
3GTOX-ray4.00E1-215[»]
3GTPX-ray3.90E1-215[»]
3GTQX-ray3.80E1-215[»]
3H3VX-ray4.00F1-215[»]
3HOUX-ray3.20E/Q1-215[»]
3HOVX-ray3.50E1-215[»]
3HOWX-ray3.60E1-215[»]
3HOXX-ray3.65E1-215[»]
3HOYX-ray3.40E1-215[»]
3HOZX-ray3.65E1-215[»]
3I4MX-ray3.70E1-215[»]
3I4NX-ray3.90E1-215[»]
3J0Kelectron microscopy36.00E1-215[»]
3J1Nelectron microscopy16.00E1-215[»]
3K1FX-ray4.30E1-215[»]
3K7AX-ray3.80E1-215[»]
3M3YX-ray3.18E1-215[»]
3M4OX-ray3.57E1-215[»]
3PO2X-ray3.30E1-215[»]
3PO3X-ray3.30E1-215[»]
3QT1X-ray4.30E1-215[»]
3RZDX-ray3.30E1-215[»]
3RZOX-ray3.00E1-215[»]
3S14X-ray2.85E1-215[»]
3S15X-ray3.30E1-215[»]
3S16X-ray3.24E1-215[»]
3S17X-ray3.20E1-215[»]
3S1MX-ray3.13E1-215[»]
3S1NX-ray3.10E1-215[»]
3S1QX-ray3.30E1-215[»]
3S1RX-ray3.20E1-215[»]
3S2DX-ray3.20E1-215[»]
3S2HX-ray3.30E1-215[»]
4A3BX-ray3.50E1-215[»]
4A3CX-ray3.50E1-215[»]
4A3DX-ray3.40E1-215[»]
4A3EX-ray3.40E1-215[»]
4A3FX-ray3.50E1-215[»]
4A3GX-ray3.50E1-215[»]
4A3IX-ray3.80E1-215[»]
4A3JX-ray3.70E1-215[»]
4A3KX-ray3.50E1-215[»]
4A3LX-ray3.50E1-215[»]
4A3MX-ray3.90E1-215[»]
4A93X-ray3.40E1-215[»]
4BBRX-ray3.40E1-215[»]
4BBSX-ray3.60E1-215[»]
4BXXX-ray3.28E1-215[»]
4BXZX-ray4.80E1-215[»]
4BY1X-ray3.60E1-215[»]
4BY7X-ray3.15E1-215[»]
4C2MX-ray2.80E/T1-215[»]
4C3HX-ray3.27E1-215[»]
4C3IX-ray3.0E1-215[»]
4C3JX-ray3.35E1-215[»]
4V1Melectron microscopy6.60E1-215[»]
4V1Nelectron microscopy7.80E1-215[»]
4V1Oelectron microscopy9.70E1-215[»]
4X67X-ray4.10E1-215[»]
4X6AX-ray3.96E1-215[»]
4Y52X-ray3.50E1-215[»]
4Y7NX-ray3.30E1-215[»]
4YM7X-ray5.50AE/BE/CE/DE/EE/FE1-215[»]
5C3EX-ray3.70E1-215[»]
5C44X-ray3.95E1-215[»]
5C4AX-ray4.20E1-215[»]
5C4JX-ray4.00E1-215[»]
5C4XX-ray4.00E1-215[»]
5FJ8electron microscopy3.90E1-215[»]
5FJ9electron microscopy4.60E1-215[»]
5FJAelectron microscopy4.65E1-215[»]
5FMFelectron microscopy6.00E2-215[»]
5FYWelectron microscopy4.35E1-215[»]
5FZ5electron microscopy8.80E1-215[»]
5G5Lelectron microscopy4.80E1-215[»]
5IP7X-ray3.52E2-215[»]
5IP9X-ray3.90E2-215[»]
5LMXelectron microscopy4.90E1-215[»]
5M3Felectron microscopy3.80E1-215[»]
5M3Melectron microscopy4.00E1-215[»]
5M5Welectron microscopy3.80E1-215[»]
5M5Xelectron microscopy4.00E1-215[»]
5M5Yelectron microscopy4.00E1-215[»]
5M64electron microscopy4.60E1-215[»]
5N5Yelectron microscopy7.70E1-215[»]
5N5Zelectron microscopy7.70E1-215[»]
5N60electron microscopy7.70E1-215[»]
5N61electron microscopy3.40E1-215[»]
5OA1electron microscopy4.40E1-215[»]
5OQJelectron microscopy4.70E1-215[»]
5OQMelectron microscopy5.80E1-215[»]
5OT2X-ray3.20E1-215[»]
5SVAelectron microscopy15.30E1-215[»]
5U5QX-ray3.80E1-215[»]
5VVRelectron microscopy5.80E1-215[»]
5VVSelectron microscopy6.40E1-215[»]
5W4UX-ray3.60E1-215[»]
5W51X-ray3.40E1-215[»]
5W5Yelectron microscopy3.80E1-215[»]
5W64electron microscopy4.20E1-215[»]
5W65electron microscopy4.30E1-215[»]
5W66electron microscopy3.90E1-215[»]
6BLOX-ray3.40E1-215[»]
6BLPX-ray3.20E1-215[»]
6BM2X-ray3.40E1-215[»]
6BM4X-ray2.95E1-215[»]
6BQFX-ray3.35E1-215[»]
6CNBelectron microscopy4.10E1-215[»]
6CNCelectron microscopy4.10E1-215[»]
6CNDelectron microscopy4.80E1-215[»]
6CNFelectron microscopy4.50E1-215[»]
6EU0electron microscopy4.00E1-215[»]
6EU1electron microscopy3.40E1-215[»]
6EU2electron microscopy3.40E1-215[»]
6EU3electron microscopy3.30E1-215[»]
6F40electron microscopy3.70E1-215[»]
6F41electron microscopy4.30E1-215[»]
6F42electron microscopy5.50E1-215[»]
6F44electron microscopy4.20E1-215[»]
6GYKelectron microscopy5.10E1-215[»]
6GYLelectron microscopy4.80E1-215[»]
6GYMelectron microscopy6.70E1-215[»]
6H67electron microscopy3.60E1-215[»]
6H68electron microscopy4.60E1-215[»]
6HKOelectron microscopy3.42E1-215[»]
6HLQelectron microscopy3.18E1-215[»]
6HLRelectron microscopy3.18E1-215[»]
6HLSelectron microscopy3.21E1-215[»]
6I84electron microscopy4.40E1-215[»]
6O6Celectron microscopy3.10D1-215[»]
6RQHelectron microscopy3.70E1-215[»]
6RQLelectron microscopy2.90E1-215[»]
6RQTelectron microscopy4.00E1-215[»]
6RRDelectron microscopy3.10E1-215[»]
6RUIelectron microscopy2.70E1-215[»]
6RUOelectron microscopy3.50E1-215[»]
6RWEelectron microscopy3.00E1-215[»]
SMRiP20434
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi32853, 276 interactors
ComplexPortaliCPX-1664 DNA-directed RNA Polymerase I complex
CPX-2660 DNA-directed RNA polymerase III complex
CPX-2662 DNA-directed RNA polymerase II complex
DIPiDIP-71N
IntActiP20434, 56 interactors
MINTiP20434
STRINGi4932.YBR154C

PTM databases

iPTMnetiP20434

Proteomic databases

MaxQBiP20434
PaxDbiP20434
PRIDEiP20434

Genome annotation databases

EnsemblFungiiYBR154C_mRNA; YBR154C; YBR154C
GeneIDi852451
KEGGisce:YBR154C

Organism-specific databases

EuPathDBiFungiDB:YBR154C
SGDiS000000358 RPB5

Phylogenomic databases

HOGENOMiCLU_058320_0_0_1
InParanoidiP20434
KOiK03013
OMAiMQMCHDR

Enzyme and pathway databases

BioCyciYEAST:G3O-29104-MONOMER
ReactomeiR-SCE-113418 Formation of the Early Elongation Complex
R-SCE-674695 RNA Polymerase II Pre-transcription Events
R-SCE-6781823 Formation of TC-NER Pre-Incision Complex
R-SCE-6782135 Dual incision in TC-NER
R-SCE-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-SCE-6796648 TP53 Regulates Transcription of DNA Repair Genes
R-SCE-6807505 RNA polymerase II transcribes snRNA genes
R-SCE-72086 mRNA Capping
R-SCE-73762 RNA Polymerase I Transcription Initiation
R-SCE-73772 RNA Polymerase I Promoter Escape
R-SCE-73776 RNA Polymerase II Promoter Escape
R-SCE-73779 RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
R-SCE-75953 RNA Polymerase II Transcription Initiation
R-SCE-75955 RNA Polymerase II Transcription Elongation
R-SCE-76042 RNA Polymerase II Transcription Initiation And Promoter Clearance
R-SCE-76061 RNA Polymerase III Transcription Initiation From Type 1 Promoter
R-SCE-76066 RNA Polymerase III Transcription Initiation From Type 2 Promoter
R-SCE-77075 RNA Pol II CTD phosphorylation and interaction with CE
R-SCE-9018519 Estrogen-dependent gene expression

Miscellaneous databases

EvolutionaryTraceiP20434

Protein Ontology

More...
PROi
PR:P20434
RNActiP20434 protein

Family and domain databases

Gene3Di3.40.1340.10, 1 hit
3.90.940.20, 1 hit
HAMAPiMF_00025 RNApol_RpoH_RPB5, 1 hit
InterProiView protein in InterPro
IPR014381 DNA_RNA_pol_RPB5_euk/virus
IPR005571 RNA_pol_Rpb5_N
IPR036710 RNA_pol_Rpb5_N_sf
IPR000783 RNA_pol_subH/Rpb5_C
IPR020608 RNA_pol_subH/Rpb5_CS
IPR039531 Rpb5-like
IPR035913 RPB5-like_sf
IPR020609 RpoH/RPB5
PANTHERiPTHR10535 PTHR10535, 1 hit
PfamiView protein in Pfam
PF01191 RNA_pol_Rpb5_C, 1 hit
PF03871 RNA_pol_Rpb5_N, 1 hit
PIRSFiPIRSF000747 RPB5, 1 hit
SUPFAMiSSF53036 SSF53036, 1 hit
SSF55287 SSF55287, 1 hit
PROSITEiView protein in PROSITE
PS01110 RNA_POL_H_23KD, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRPAB1_YEAST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P20434
Secondary accession number(s): D6VQE9, Q02121
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 22, 2020
This is version 206 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

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