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UniProtKB - P22139 (RPAB5_YEAST)

Entry version 208 (29 Sep 2021)
Sequence version 2 (01 Oct 1993)
Previous versions | rss
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Protein

DNA-directed RNA polymerases I, II, and III subunit RPABC5

Gene

RPB10

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 a small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, RBP10 is part of the core element with the central large cleft.

3 Publications

Miscellaneous

Present with 5300 molecules/cell in log phase SD medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi7ZincCombined sources1 Publication1
Metal bindingi10ZincCombined sources1 Publication1
Metal bindingi45ZincCombined sources1 Publication1
Metal bindingi46ZincCombined sources1 Publication1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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
LigandMetal-binding, Zinc

Enzyme and pathway databases

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_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 RPABC5
Short name:
RNA polymerases I, II, and III subunit ABC5
Alternative name(s):
ABC10-beta
ABC8
DNA-directed RNA polymerases I, II, and III 8.3 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:RPB10
Ordered Locus Names:YOR210W
<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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<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 XV

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000005736, RPB10

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YOR210W

<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

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_00001213421 – 70DNA-directed RNA polymerases I, II, and III subunit RPABC5Add BLAST70

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki59Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P22139

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

More...PaxDbi		P22139

PRoteomics IDEntifications database

More...PRIDEi		P22139

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P22139

<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.

6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		34605, 447 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

More...DIPi		DIP-825N

Protein interaction database and analysis system

More...IntActi		P22139, 27 interactors

Molecular INTeraction database

More...MINTi		P22139

STRING: functional protein association networks

More...STRINGi		4932.YOR210W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P22139, 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

170
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

More...SMRi		P22139

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P22139

<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

Belongs to the archaeal Rpo10/eukaryotic RPB10 RNA polymerase subunit family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3497, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00390000007087

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_143122_2_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P22139

Identification of Orthologs from Complete Genome Data

More...OMAi		YCCRRMF

Family and domain databases

HAMAP database of protein families

More...HAMAPi		MF_00250, RNApol_arch_Rpo10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR023580, RNA_pol_su_RPB10
IPR020789, RNA_pol_suN_Zn-BS
IPR000268, RNAP_N/Rpb10

The PANTHER Classification System

More...PANTHERi		PTHR23431, PTHR23431, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01194, RNA_pol_N, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF005653, RNA_pol_N/8_sub, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF46924, SSF46924, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS01112, RNA_POL_N_8KD, 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>. 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_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.

P22139-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIVPVRCFSC GKVVGDKWES YLNLLQEDEL DEGTALSRLG LKRYCCRRMI 
        60         70
LTHVDLIEKF LRYNPLEKRD
Length:70
Mass (Da):8,278
Last modified:October 1, 1993 - v2
<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:iE1F5733E8F466BE0
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M60479 Genomic DNA Translation: AAA34995.1 Sequence problems.
S62098 Genomic DNA Translation: AAB27020.1
L11274 Genomic DNA Translation: AAB59318.1
Z75118 Genomic DNA Translation: CAA99425.1
AY558433 Genomic DNA Translation: AAS56759.1
BK006948 Genomic DNA Translation: DAA10982.1

Protein sequence database of the Protein Information Resource

More...PIRi		S48885

NCBI Reference Sequences

More...RefSeqi		NP_014853.3, NM_001183629.3

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YOR210W_mRNA; YOR210W; YOR210W

Database of genes from NCBI RefSeq genomes

More...GeneIDi		854385

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YOR210W

<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
M60479 Genomic DNA Translation: AAA34995.1 Sequence problems.
S62098 Genomic DNA Translation: AAB27020.1
L11274 Genomic DNA Translation: AAB59318.1
Z75118 Genomic DNA Translation: CAA99425.1
AY558433 Genomic DNA Translation: AAS56759.1
BK006948 Genomic DNA Translation: DAA10982.1
PIRiS48885
RefSeqiNP_014853.3, NM_001183629.3

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-ray3.10J1-70[»]
1I50X-ray2.80J1-70[»]
1I6HX-ray3.30J1-70[»]
1K83X-ray2.80J1-70[»]
1NIKX-ray4.10J1-70[»]
1NT9X-ray4.20J1-70[»]
1PQVX-ray3.80J1-70[»]
1R5UX-ray4.50J1-70[»]
1R9SX-ray4.25J1-70[»]
1R9TX-ray3.50J1-70[»]
1SFOX-ray3.61J1-70[»]
1TWAX-ray3.20J1-70[»]
1TWCX-ray3.00J1-70[»]
1TWFX-ray2.30J1-70[»]
1TWGX-ray3.30J1-70[»]
1TWHX-ray3.40J1-70[»]
1WCMX-ray3.80J1-70[»]
1Y1VX-ray3.80J1-70[»]
1Y1WX-ray4.00J1-70[»]
1Y1YX-ray4.00J1-70[»]
1Y77X-ray4.50J1-70[»]
2B63X-ray3.80J1-70[»]
2B8KX-ray4.15J1-70[»]
2E2HX-ray3.95J1-70[»]
2E2IX-ray3.41J1-70[»]
2E2JX-ray3.50J1-70[»]
2JA5X-ray3.80J1-70[»]
2JA6X-ray4.00J1-70[»]
2JA7X-ray3.80J/V1-70[»]
2JA8X-ray3.80J1-70[»]
2NVQX-ray2.90J1-70[»]
2NVTX-ray3.36J1-70[»]
2NVXX-ray3.60J1-70[»]
2NVYX-ray3.40J1-70[»]
2NVZX-ray4.30J1-70[»]
2R7ZX-ray3.80J1-70[»]
2R92X-ray3.80J1-70[»]
2R93X-ray4.00J1-70[»]
2VUMX-ray3.40J1-70[»]
2YU9X-ray3.40J1-70[»]
3CQZX-ray2.80J1-70[»]
3FKIX-ray3.88J1-70[»]
3GTGX-ray3.78J1-70[»]
3GTJX-ray3.42J1-70[»]
3GTKX-ray3.80J1-70[»]
3GTLX-ray3.38J1-70[»]
3GTMX-ray3.80J1-70[»]
3GTOX-ray4.00J1-70[»]
3GTPX-ray3.90J1-70[»]
3GTQX-ray3.80J1-70[»]
3H3VX-ray4.00K1-70[»]
3HOUX-ray3.20J/V1-70[»]
3HOVX-ray3.50J1-70[»]
3HOWX-ray3.60J1-70[»]
3HOXX-ray3.65J1-70[»]
3HOYX-ray3.40J1-70[»]
3HOZX-ray3.65J1-70[»]
3I4MX-ray3.70J1-70[»]
3I4NX-ray3.90J1-70[»]
3J0Kelectron microscopy36.00J1-70[»]
3J1Nelectron microscopy16.00J1-70[»]
3K1FX-ray4.30J1-70[»]
3K7AX-ray3.80J1-70[»]
3M3YX-ray3.18J1-70[»]
3M4OX-ray3.57J1-70[»]
3PO2X-ray3.30J1-70[»]
3PO3X-ray3.30J1-70[»]
3QT1X-ray4.30J1-70[»]
3RZDX-ray3.30J1-70[»]
3RZOX-ray3.00J1-70[»]
3S14X-ray2.85J1-70[»]
3S15X-ray3.30J1-70[»]
3S16X-ray3.24J1-70[»]
3S17X-ray3.20J1-70[»]
3S1MX-ray3.13J1-70[»]
3S1NX-ray3.10J1-70[»]
3S1QX-ray3.30J1-70[»]
3S1RX-ray3.20J1-70[»]
3S2DX-ray3.20J1-70[»]
3S2HX-ray3.30J1-70[»]
4A3BX-ray3.50J1-70[»]
4A3CX-ray3.50J1-70[»]
4A3DX-ray3.40J1-70[»]
4A3EX-ray3.40J1-70[»]
4A3FX-ray3.50J1-70[»]
4A3GX-ray3.50J1-70[»]
4A3IX-ray3.80J1-70[»]
4A3JX-ray3.70J1-70[»]
4A3KX-ray3.50J1-70[»]
4A3LX-ray3.50J1-70[»]
4A3MX-ray3.90J1-70[»]
4A93X-ray3.40J1-70[»]
4BBRX-ray3.40J1-70[»]
4BBSX-ray3.60J1-70[»]
4BXXX-ray3.28J1-70[»]
4BXZX-ray4.80J1-70[»]
4BY1X-ray3.60J1-70[»]
4BY7X-ray3.15J1-70[»]
4C2MX-ray2.80J/Y1-70[»]
4C3HX-ray3.27J1-70[»]
4C3IX-ray3.0J1-70[»]
4C3JX-ray3.35J1-70[»]
4V1Melectron microscopy6.60J1-70[»]
4V1Nelectron microscopy7.80J1-70[»]
4V1Oelectron microscopy9.70J1-70[»]
4X67X-ray4.10J1-70[»]
4X6AX-ray3.96J1-70[»]
4Y52X-ray3.50J1-70[»]
4Y7NX-ray3.30J1-70[»]
4YM7X-ray5.50AJ/BJ/CJ/DJ/EJ/FJ1-70[»]
5C3EX-ray3.70J1-70[»]
5C44X-ray3.95J1-70[»]
5C4AX-ray4.20J1-70[»]
5C4JX-ray4.00J1-70[»]
5C4XX-ray4.00J1-70[»]
5FJ8electron microscopy3.90J1-70[»]
5FJ9electron microscopy4.60J1-70[»]
5FJAelectron microscopy4.65J1-70[»]
5FMFelectron microscopy6.00J1-65[»]
5FYWelectron microscopy4.35J1-70[»]
5FZ5electron microscopy8.80J1-70[»]
5G5Lelectron microscopy4.80J1-70[»]
5IP7X-ray3.52J1-65[»]
5IP9X-ray3.90J1-65[»]
5LMXelectron microscopy4.90J1-70[»]
5M3Felectron microscopy3.80J1-70[»]
5M3Melectron microscopy4.00J1-70[»]
5M5Welectron microscopy3.80J1-70[»]
5M5Xelectron microscopy4.00J1-70[»]
5M5Yelectron microscopy4.00J1-70[»]
5M64electron microscopy4.60J1-70[»]
5N5Yelectron microscopy7.70J1-70[»]
5N5Zelectron microscopy7.70J1-70[»]
5N60electron microscopy7.70J1-70[»]
5N61electron microscopy3.40J1-70[»]
5OA1electron microscopy4.40J1-70[»]
5OQJelectron microscopy4.70J1-70[»]
5OQMelectron microscopy5.80J1-70[»]
5OT2X-ray3.20J1-70[»]
5SVAelectron microscopy15.30J1-70[»]
5U5QX-ray3.80J1-70[»]
5VVRelectron microscopy5.80J1-70[»]
5VVSelectron microscopy6.40J1-70[»]
5W4UX-ray3.60J1-70[»]
5W51X-ray3.40J1-70[»]
5W5Yelectron microscopy3.80J1-70[»]
5W64electron microscopy4.20J1-70[»]
5W65electron microscopy4.30J1-70[»]
5W66electron microscopy3.90J1-70[»]
6BLOX-ray3.40J1-70[»]
6BLPX-ray3.20J1-70[»]
6BM2X-ray3.40J1-70[»]
6BM4X-ray2.95J1-70[»]
6BQFX-ray3.35J1-70[»]
6CNBelectron microscopy4.10J1-70[»]
6CNCelectron microscopy4.10J1-70[»]
6CNDelectron microscopy4.80J1-70[»]
6CNFelectron microscopy4.50J1-70[»]
6EU0electron microscopy4.00J1-70[»]
6EU1electron microscopy3.40J1-70[»]
6EU2electron microscopy3.40J1-70[»]
6EU3electron microscopy3.30J1-70[»]
6F40electron microscopy3.70J1-70[»]
6F41electron microscopy4.30J1-70[»]
6F42electron microscopy5.50J1-70[»]
6F44electron microscopy4.20J1-70[»]
6GYKelectron microscopy5.10J1-70[»]
6GYLelectron microscopy4.80J1-70[»]
6GYMelectron microscopy6.70J1-70[»]
6H67electron microscopy3.60J1-70[»]
6H68electron microscopy4.60J1-70[»]
6HKOelectron microscopy3.42J1-70[»]
6HLQelectron microscopy3.18J1-70[»]
6HLRelectron microscopy3.18J1-70[»]
6HLSelectron microscopy3.21J1-70[»]
6I84electron microscopy4.40J1-70[»]
6O6Celectron microscopy3.10H1-70[»]
6RQHelectron microscopy3.70J1-70[»]
6RQLelectron microscopy2.90J1-70[»]
6RQTelectron microscopy4.00J1-70[»]
6RRDelectron microscopy3.10J1-70[»]
6RUIelectron microscopy2.70J1-70[»]
6RUOelectron microscopy3.50J1-70[»]
6RWEelectron microscopy3.00J1-70[»]
6TPSelectron microscopy3.54J1-70[»]
6TUTelectron microscopy3.25J1-70[»]
6UPXX-ray3.40J1-70[»]
6UPYX-ray3.40J1-70[»]
6UPZX-ray3.10J1-70[»]
6UQ0X-ray3.56J1-70[»]
6UQ1X-ray3.60J1-70[»]
6UQ2X-ray3.20J1-70[»]
6UQ3X-ray3.47J1-70[»]
7KEDX-ray3.60J1-70[»]
7KEEX-ray3.45J1-70[»]
7KEFX-ray3.89J1-70[»]
7O4Ielectron microscopy3.20J1-70[»]
7O4Jelectron microscopy2.90J1-70[»]
7O72electron microscopy3.40J1-70[»]
7O73electron microscopy3.40J1-70[»]
7O75electron microscopy3.20J1-70[»]
SMRiP22139
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi34605, 447 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-825N
IntActiP22139, 27 interactors
MINTiP22139
STRINGi4932.YOR210W

PTM databases

iPTMnetiP22139

Proteomic databases

MaxQBiP22139
PaxDbiP22139
PRIDEiP22139

Genome annotation databases

EnsemblFungiiYOR210W_mRNA; YOR210W; YOR210W
GeneIDi854385
KEGGisce:YOR210W

Organism-specific databases

SGDiS000005736, RPB10
VEuPathDBiFungiDB:YOR210W

Phylogenomic databases

eggNOGiKOG3497, Eukaryota
GeneTreeiENSGT00390000007087
HOGENOMiCLU_143122_2_1_1
InParanoidiP22139
OMAiYCCRRMF

Enzyme and pathway databases

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

EvolutionaryTraceiP22139

Protein Ontology

More...PROi		PR:P22139
RNActiP22139, protein

Family and domain databases

HAMAPiMF_00250, RNApol_arch_Rpo10, 1 hit
InterProiView protein in InterPro
IPR023580, RNA_pol_su_RPB10
IPR020789, RNA_pol_suN_Zn-BS
IPR000268, RNAP_N/Rpb10
PANTHERiPTHR23431, PTHR23431, 1 hit
PfamiView protein in Pfam
PF01194, RNA_pol_N, 1 hit
PIRSFiPIRSF005653, RNA_pol_N/8_sub, 1 hit
SUPFAMiSSF46924, SSF46924, 1 hit
PROSITEiView protein in PROSITE
PS01112, RNA_POL_N_8KD, 1 hit

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 nameiRPAB5_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: P22139
Secondary accession number(s): D6W2R6
<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: August 1, 1991
Last sequence update: October 1, 1993
Last modified: September 29, 2021
This is version 208 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

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