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Protein

DNA-directed RNA polymerases I, II, and III subunit RPABC2

Gene

RPO26

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 polymerases are composed of mobile elements that move relative to each other. In Pol II, RPB6 is part of the clamp element and together with parts of RPB1 and RPB2 forms a pocket to which the RPB4-RPB7 subcomplex binds.3 Publications

Miscellaneous

Present with 6090 molecules/cell in log phase SD medium.1 Publication

<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

  • DNA binding Source: InterPro
  • RNA polymerase I activity Source: UniProtKB

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

Biological processRibosome biogenesis, Transcription

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
YEAST:G3O-34310-MONOMER

Reactome - a knowledgebase of biological pathways and processes

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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-72165 mRNA Splicing - Minor Pathway
R-SCE-73762 RNA Polymerase I Transcription Initiation
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-76042 RNA Polymerase II Transcription Initiation And Promoter Clearance
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_and_taxonomy_section">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 RPABC2
Short name:
RNA polymerases I, II, and III subunit ABC2
Alternative name(s):
ABC23
DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:RPO26
Synonyms:RPB6
Ordered Locus Names:YPR187W
ORF Names:P9677.8
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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 XVI

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000006391 RPO26

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001337971 – 155DNA-directed RNA polymerases I, II, and III subunit RPABC2Add BLAST155

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei24PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P20435

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

More...
PaxDbi
P20435

PRoteomics IDEntifications database

More...
PRIDEi
P20435

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P20435

<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_section">'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_section">'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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
36359, 104 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
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-2194N

Protein interaction database and analysis system

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IntActi
P20435, 41 interactors

Molecular INTeraction database

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MINTi
P20435

STRING: functional protein association networks

More...
STRINGi
4932.YPR187W

<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

1155
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Database of protein disorder

More...
DisProti
DP00771

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P20435

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

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SMRi
P20435

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P20435

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni111 – 132Leucine-zipperAdd BLAST22

<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

Ensembl GeneTree

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GeneTreei
ENSGT00390000010415

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000225272

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P20435

KEGG Orthology (KO)

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KOi
K03014

Identification of Orthologs from Complete Genome Data

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OMAi
RTIVNGG

Database of Orthologous Groups

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OrthoDBi
EOG092C5A9A

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.90.940.10, 1 hit

HAMAP database of protein families

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HAMAPi
MF_00192 RNApol_arch_K, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR020708 DNA-dir_RNA_polK_14-18kDa_CS
IPR006110 Pol_omega/K/RPB6
IPR012293 RNAP_RPB6_omega
IPR028363 RPB6
IPR036161 RPB6/omega_like_sf
IPR006111 RpoK/Rpb6

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01192 RNA_pol_Rpb6, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF500154 RPB6, 1 hit
PIRSF000778 RpoK/RPB6, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01409 RNA_pol_Rpb6, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF63562 SSF63562, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01111 RNA_POL_K_14KD, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P20435-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSDYEEAFND GNENFEDFDV EHFSDEETYE EKPQFKDGET TDANGKTIVT
60 70 80 90 100
GGNGPEDFQQ HEQIRRKTLK EKAIPKDQRA TTPYMTKYER ARILGTRALQ
110 120 130 140 150
ISMNAPVFVD LEGETDPLRI AMKELAEKKI PLVIRRYLPD GSFEDWSVEE

LIVDL
Length:155
Mass (Da):17,910
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:iAA3DEF529F94A5E4
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X53288 Genomic DNA Translation: CAA37382.1
M33924 Genomic DNA Translation: AAA34989.1
U25841 Genomic DNA Translation: AAB64616.1
BK006949 Genomic DNA Translation: DAA11603.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S13307 RNBYR6

NCBI Reference Sequences

More...
RefSeqi
NP_015513.1, NM_001184284.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YPR187W_mRNA; YPR187W_mRNA; YPR187W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
856317

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YPR187W

<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
X53288 Genomic DNA Translation: CAA37382.1
M33924 Genomic DNA Translation: AAA34989.1
U25841 Genomic DNA Translation: AAB64616.1
BK006949 Genomic DNA Translation: DAA11603.1
PIRiS13307 RNBYR6
RefSeqiNP_015513.1, NM_001184284.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I3QX-ray3.10F1-155[»]
1I50X-ray2.80F1-155[»]
1I6HX-ray3.30F1-155[»]
1K83X-ray2.80F1-155[»]
1NIKX-ray4.10F1-155[»]
1NT9X-ray4.20F1-155[»]
1PQVX-ray3.80F1-155[»]
1R5UX-ray4.50F1-155[»]
1R9SX-ray4.25F1-155[»]
1R9TX-ray3.50F1-155[»]
1SFOX-ray3.61F1-155[»]
1TWAX-ray3.20F1-155[»]
1TWCX-ray3.00F1-155[»]
1TWFX-ray2.30F1-155[»]
1TWGX-ray3.30F1-155[»]
1TWHX-ray3.40F1-155[»]
1WCMX-ray3.80F1-155[»]
1Y1VX-ray3.80F1-155[»]
1Y1WX-ray4.00F1-155[»]
1Y1YX-ray4.00F1-155[»]
1Y77X-ray4.50F1-155[»]
2B63X-ray3.80F1-155[»]
2B8KX-ray4.15F1-155[»]
2E2HX-ray3.95F1-155[»]
2E2IX-ray3.41F1-155[»]
2E2JX-ray3.50F1-155[»]
2JA5X-ray3.80F1-155[»]
2JA6X-ray4.00F1-155[»]
2JA7X-ray3.80F/R1-155[»]
2JA8X-ray3.80F1-155[»]
2NVQX-ray2.90F1-155[»]
2NVTX-ray3.36F1-155[»]
2NVXX-ray3.60F1-155[»]
2NVYX-ray3.40F1-155[»]
2NVZX-ray4.30F1-155[»]
2R7ZX-ray3.80F1-155[»]
2R92X-ray3.80F1-155[»]
2R93X-ray4.00F1-155[»]
2VUMX-ray3.40F1-155[»]
2YU9X-ray3.40F1-155[»]
3CQZX-ray2.80F1-155[»]
3FKIX-ray3.88F1-155[»]
3GTGX-ray3.78F1-155[»]
3GTJX-ray3.42F1-155[»]
3GTKX-ray3.80F1-155[»]
3GTLX-ray3.38F1-155[»]
3GTMX-ray3.80F1-155[»]
3GTOX-ray4.00F1-155[»]
3GTPX-ray3.90F1-155[»]
3GTQX-ray3.80F1-155[»]
3H3VX-ray4.00G1-155[»]
3HOUX-ray3.20F/R1-155[»]
3HOVX-ray3.50F1-155[»]
3HOWX-ray3.60F1-155[»]
3HOXX-ray3.65F1-155[»]
3HOYX-ray3.40F1-155[»]
3HOZX-ray3.65F1-155[»]
3I4MX-ray3.70F1-155[»]
3I4NX-ray3.90F1-155[»]
3J0Kelectron microscopy36.00F72-155[»]
3J1Nelectron microscopy16.00F72-155[»]
3K1FX-ray4.30F1-155[»]
3K7AX-ray3.80F1-155[»]
3M3YX-ray3.18F1-155[»]
3M4OX-ray3.57F1-155[»]
3PO2X-ray3.30F1-155[»]
3PO3X-ray3.30F1-155[»]
3QT1X-ray4.30F1-155[»]
3RZDX-ray3.30F1-155[»]
3RZOX-ray3.00F1-155[»]
3S14X-ray2.85F1-155[»]
3S15X-ray3.30F1-155[»]
3S16X-ray3.24F1-155[»]
3S17X-ray3.20F1-155[»]
3S1MX-ray3.13F1-155[»]
3S1NX-ray3.10F1-155[»]
3S1QX-ray3.30F1-155[»]
3S1RX-ray3.20F1-155[»]
3S2DX-ray3.20F1-155[»]
3S2HX-ray3.30F1-155[»]
4A3BX-ray3.50F1-155[»]
4A3CX-ray3.50F1-155[»]
4A3DX-ray3.40F1-155[»]
4A3EX-ray3.40F1-155[»]
4A3FX-ray3.50F1-155[»]
4A3GX-ray3.50F1-155[»]
4A3IX-ray3.80F1-155[»]
4A3JX-ray3.70F1-155[»]
4A3KX-ray3.50F1-155[»]
4A3LX-ray3.50F1-155[»]
4A3MX-ray3.90F1-155[»]
4A93X-ray3.40F1-155[»]
4BBRX-ray3.40F1-155[»]
4BBSX-ray3.60F1-155[»]
4BXXX-ray3.28F1-155[»]
4BXZX-ray4.80F1-155[»]
4BY1X-ray3.60F1-155[»]
4BY7X-ray3.15F1-155[»]
4C2MX-ray2.80F/U1-155[»]
4C3HX-ray3.27F1-155[»]
4C3IX-ray3.0F1-155[»]
4C3JX-ray3.35F1-155[»]
4V1Melectron microscopy6.60F1-155[»]
4V1Nelectron microscopy7.80F1-155[»]
4V1Oelectron microscopy9.70F1-155[»]
4X67X-ray4.10F1-155[»]
4X6AX-ray3.96F1-155[»]
4Y52X-ray3.50F1-155[»]
4Y7NX-ray3.30F1-155[»]
4YM7X-ray5.50AF/BF/CF/DF/EF/FF1-155[»]
5C3EX-ray3.70F1-155[»]
5C44X-ray3.95F1-155[»]
5C4AX-ray4.20F1-155[»]
5C4JX-ray4.00F1-155[»]
5C4XX-ray4.00F1-155[»]
5FJ8electron microscopy3.90F1-155[»]
5FJ9electron microscopy4.60F1-155[»]
5FJAelectron microscopy4.65F1-155[»]
5FMFelectron microscopy6.00F72-155[»]
5FYWelectron microscopy4.35F1-155[»]
5FZ5electron microscopy8.80F1-155[»]
5G5Lelectron microscopy4.80F1-155[»]
5IP7X-ray3.52F69-155[»]
5IP9X-ray3.90F69-155[»]
5LMXelectron microscopy4.90F1-155[»]
5M3Felectron microscopy3.80F1-155[»]
5M3Melectron microscopy4.00F1-155[»]
5M5Welectron microscopy3.80F1-155[»]
5M5Xelectron microscopy4.00F1-155[»]
5M5Yelectron microscopy4.00F1-155[»]
5M64electron microscopy4.60F1-155[»]
5N5Yelectron microscopy7.70F1-155[»]
5N5Zelectron microscopy7.70F1-155[»]
5N60electron microscopy7.70F1-155[»]
5N61electron microscopy3.40F1-155[»]
5OA1electron microscopy4.40F1-155[»]
5OQJelectron microscopy4.70F1-155[»]
5OQMelectron microscopy5.80F1-155[»]
5OT2X-ray3.20F1-155[»]
5SVAelectron microscopy15.30F1-155[»]
5U5QX-ray3.80F1-155[»]
5VVRelectron microscopy5.80F1-155[»]
5VVSelectron microscopy6.40F1-155[»]
5W4UX-ray3.60F1-155[»]
5W51X-ray3.40F1-155[»]
5W5Yelectron microscopy3.80F1-155[»]
5W64electron microscopy4.20F1-155[»]
5W65electron microscopy4.30F1-155[»]
5W66electron microscopy3.90F1-155[»]
6BLOX-ray3.40F1-155[»]
6BLPX-ray3.20F1-155[»]
6BM2X-ray3.40F1-155[»]
6BM4X-ray2.95F1-155[»]
6BQFX-ray3.35F1-155[»]
6CNBelectron microscopy4.10F1-155[»]
6CNCelectron microscopy4.10F1-155[»]
6CNDelectron microscopy4.80F1-155[»]
6CNFelectron microscopy4.50F1-155[»]
6EU0electron microscopy4.00F1-155[»]
6EU1electron microscopy3.40F1-155[»]
6EU2electron microscopy3.40F1-155[»]
6EU3electron microscopy3.30F1-155[»]
6F40electron microscopy3.70F1-155[»]
6F41electron microscopy4.30F1-155[»]
6F42electron microscopy5.50F1-155[»]
6F44electron microscopy4.20F1-155[»]
6H67electron microscopy3.60F1-155[»]
6H68electron microscopy4.60F1-155[»]
DisProtiDP00771
ProteinModelPortaliP20435
SMRiP20435
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36359, 104 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-2194N
IntActiP20435, 41 interactors
MINTiP20435
STRINGi4932.YPR187W

PTM databases

iPTMnetiP20435

Proteomic databases

MaxQBiP20435
PaxDbiP20435
PRIDEiP20435

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR187W_mRNA; YPR187W_mRNA; YPR187W
GeneIDi856317
KEGGisce:YPR187W

Organism-specific databases

SGDiS000006391 RPO26

Phylogenomic databases

GeneTreeiENSGT00390000010415
HOGENOMiHOG000225272
InParanoidiP20435
KOiK03014
OMAiRTIVNGG
OrthoDBiEOG092C5A9A

Enzyme and pathway databases

BioCyciYEAST:G3O-34310-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-72165 mRNA Splicing - Minor Pathway
R-SCE-73762 RNA Polymerase I Transcription Initiation
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-76042 RNA Polymerase II Transcription Initiation And Promoter Clearance
R-SCE-77075 RNA Pol II CTD phosphorylation and interaction with CE
R-SCE-9018519 Estrogen-dependent gene expression

Miscellaneous databases

EvolutionaryTraceiP20435

Protein Ontology

More...
PROi
PR:P20435

Family and domain databases

Gene3Di3.90.940.10, 1 hit
HAMAPiMF_00192 RNApol_arch_K, 1 hit
InterProiView protein in InterPro
IPR020708 DNA-dir_RNA_polK_14-18kDa_CS
IPR006110 Pol_omega/K/RPB6
IPR012293 RNAP_RPB6_omega
IPR028363 RPB6
IPR036161 RPB6/omega_like_sf
IPR006111 RpoK/Rpb6
PfamiView protein in Pfam
PF01192 RNA_pol_Rpb6, 1 hit
PIRSFiPIRSF500154 RPB6, 1 hit
PIRSF000778 RpoK/RPB6, 1 hit
SMARTiView protein in SMART
SM01409 RNA_pol_Rpb6, 1 hit
SUPFAMiSSF63562 SSF63562, 1 hit
PROSITEiView protein in PROSITE
PS01111 RNA_POL_K_14KD, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiRPAB2_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: P20435
Secondary accession number(s): D6W4I7
<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_and_isoforms">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: December 5, 2018
This is version 198 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, Complete proteome, Reference proteome

Documents

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