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Entry version 191 (31 Jul 2019)
Sequence version 1 (01 Feb 1995)
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Protein

DNA-directed RNA polymerases I, II, and III subunit RPABC4

Gene

RPC10

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. RNA polymerases are composed of mobile elements that move relative to each other. In Pol II, the core element with the central large cleft comprises RPB3, RBP10, RPB11, RPB12 and regions of RPB1 and RPB2 forming the active center.3 Publications

Miscellaneous

Present with 907 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 bindingi31Zinc1
Metal bindingi34Zinc1
Metal bindingi48Zinc1
Metal bindingi51Zinc1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri31 – 51C4-typeAdd BLAST21

<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

Biological processRibosome biogenesis, Transcription
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
YEAST:G3O-31179-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_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 RPABC4
Short name:
RNA polymerases I, II, and III subunit ABC4
Alternative name(s):
ABC10-alpha
<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:RPC10
Synonyms:RPB12
Ordered Locus Names:YHR143W-A
ORF Names:YHR143BW
<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 VIII

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
FungiDB:YHR143W-A

Saccharomyces Genome Database

More...
SGDi
S000001185 RPC10

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001597531 – 70DNA-directed RNA polymerases I, II, and III subunit RPABC4Add BLAST70

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P40422

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

More...
PaxDbi
P40422

PRoteomics IDEntifications database

More...
PRIDEi
P40422

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P40422

<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.

Interacts, via its C-terminus, with TFIIIC subunit TFC4.

7 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
36577, 72 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-936N

Protein interaction database and analysis system

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IntActi
P40422, 15 interactors

Molecular INTeraction database

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MINTi
P40422

STRING: functional protein association networks

More...
STRINGi
4932.YHR143W-A

<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

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SMRi
P40422

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P40422

<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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri31 – 51C4-typeAdd BLAST21

Keywords - Domaini

Zinc-finger

Phylogenomic databases

Ensembl GeneTree

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GeneTreei
ENSGT00940000169869

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000191755

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P40422

KEGG Orthology (KO)

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KOi
K03009

Identification of Orthologs from Complete Genome Data

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OMAi
KYICAEC

Family and domain databases

Database of protein disorder

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DisProti
DP00818

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR006591 RNAP_P/RPABC4
IPR039747 RPABC4
IPR029040 RPABC4/Spt4

The PANTHER Classification System

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PANTHERi
PTHR12056 PTHR12056, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF03604 DNA_RNApol_7kD, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00659 RPOLCX, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF63393 SSF63393, 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.

P40422-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSREGFQIPT NLDAAAAGTS QARTATLKYI CAECSSKLSL SRTDAVRCKD
60 70
CGHRILLKAR TKRLVQFEAR
Length:70
Mass (Da):7,716
Last modified:February 1, 1995 - 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:i066A3D982EC7361E
GO

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

More...
DDBJi
Links Updated
U23378 Genomic DNA Translation: AAA64417.1
U10397 Genomic DNA Translation: AAB68994.1
AY558549 Genomic DNA Translation: AAS56875.1
BK006934 Genomic DNA Translation: DAA06837.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S58932

NCBI Reference Sequences

More...
RefSeqi
NP_012013.1, NM_001179273.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YHR143W-A_mRNA; YHR143W-A_mRNA; YHR143W-A

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
856547

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YHR143W-A

<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
U23378 Genomic DNA Translation: AAA64417.1
U10397 Genomic DNA Translation: AAB68994.1
AY558549 Genomic DNA Translation: AAS56875.1
BK006934 Genomic DNA Translation: DAA06837.1
PIRiS58932
RefSeqiNP_012013.1, NM_001179273.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I3QX-ray3.10L1-70[»]
1I50X-ray2.80L1-70[»]
1I6HX-ray3.30L1-70[»]
1K83X-ray2.80L1-70[»]
1NIKX-ray4.10L1-70[»]
1NT9X-ray4.20L1-70[»]
1PQVX-ray3.80L1-70[»]
1R5UX-ray4.50L1-70[»]
1R9SX-ray4.25L1-70[»]
1R9TX-ray3.50L1-70[»]
1SFOX-ray3.61L1-70[»]
1TWAX-ray3.20L1-70[»]
1TWCX-ray3.00L1-70[»]
1TWFX-ray2.30L1-70[»]
1TWGX-ray3.30L1-70[»]
1TWHX-ray3.40L1-70[»]
1WCMX-ray3.80L1-70[»]
1Y1VX-ray3.80L1-70[»]
1Y1WX-ray4.00L1-70[»]
1Y1YX-ray4.00L1-70[»]
1Y77X-ray4.50L1-70[»]
2B63X-ray3.80L1-70[»]
2B8KX-ray4.15L1-70[»]
2E2HX-ray3.95L1-70[»]
2E2IX-ray3.41L1-70[»]
2E2JX-ray3.50L1-70[»]
2JA5X-ray3.80L1-70[»]
2JA6X-ray4.00L1-70[»]
2JA7X-ray3.80L/X1-70[»]
2JA8X-ray3.80L1-70[»]
2NVQX-ray2.90L1-70[»]
2NVTX-ray3.36L1-70[»]
2NVXX-ray3.60L1-70[»]
2NVYX-ray3.40L1-70[»]
2NVZX-ray4.30L1-70[»]
2R7ZX-ray3.80L1-70[»]
2R92X-ray3.80L1-70[»]
2R93X-ray4.00L1-70[»]
2VUMX-ray3.40L1-70[»]
2YU9X-ray3.40L1-70[»]
3CQZX-ray2.80L1-70[»]
3FKIX-ray3.88L1-70[»]
3GTGX-ray3.78L1-70[»]
3GTJX-ray3.42L1-70[»]
3GTKX-ray3.80L1-70[»]
3GTLX-ray3.38L1-70[»]
3GTMX-ray3.80L1-70[»]
3GTOX-ray4.00L1-70[»]
3GTPX-ray3.90L1-70[»]
3GTQX-ray3.80L1-70[»]
3H3VX-ray4.00M1-70[»]
3HOUX-ray3.20L/X1-70[»]
3HOVX-ray3.50L1-70[»]
3HOWX-ray3.60L1-70[»]
3HOXX-ray3.65L1-70[»]
3HOYX-ray3.40L1-70[»]
3HOZX-ray3.65L1-70[»]
3I4MX-ray3.70L1-70[»]
3I4NX-ray3.90L1-70[»]
3J1Nelectron microscopy16.00L1-70[»]
3K1FX-ray4.30L1-70[»]
3K7AX-ray3.80L1-70[»]
3M3YX-ray3.18L1-70[»]
3M4OX-ray3.57L1-70[»]
3PO2X-ray3.30L1-70[»]
3PO3X-ray3.30L1-70[»]
3QT1X-ray4.30L1-70[»]
3RZDX-ray3.30L1-70[»]
3RZOX-ray3.00L1-70[»]
3S14X-ray2.85L1-70[»]
3S15X-ray3.30L1-70[»]
3S16X-ray3.24L1-70[»]
3S17X-ray3.20L1-70[»]
3S1MX-ray3.13L1-70[»]
3S1NX-ray3.10L1-70[»]
3S1QX-ray3.30L1-70[»]
3S1RX-ray3.20L1-70[»]
3S2DX-ray3.20L1-70[»]
3S2HX-ray3.30L1-70[»]
4A3BX-ray3.50L1-70[»]
4A3CX-ray3.50L1-70[»]
4A3DX-ray3.40L1-70[»]
4A3EX-ray3.40L1-70[»]
4A3FX-ray3.50L1-70[»]
4A3GX-ray3.50L1-70[»]
4A3IX-ray3.80L1-70[»]
4A3JX-ray3.70L1-70[»]
4A3KX-ray3.50L1-70[»]
4A3LX-ray3.50L1-70[»]
4A3MX-ray3.90L1-70[»]
4A93X-ray3.40L1-70[»]
4BBRX-ray3.40L1-70[»]
4BBSX-ray3.60L1-70[»]
4BXXX-ray3.28L1-70[»]
4BXZX-ray4.80L1-70[»]
4BY1X-ray3.60L1-70[»]
4BY7X-ray3.15L1-70[»]
4C2MX-ray2.801/L1-70[»]
4C3HX-ray3.27L1-70[»]
4C3IX-ray3.0L1-70[»]
4C3JX-ray3.35L1-70[»]
4V1Melectron microscopy6.60L1-70[»]
4V1Nelectron microscopy7.80L1-70[»]
4V1Oelectron microscopy9.70L1-70[»]
4X67X-ray4.10L1-70[»]
4X6AX-ray3.96L1-70[»]
4Y52X-ray3.50L1-70[»]
4Y7NX-ray3.30L1-70[»]
4YM7X-ray5.50AL/BL/CL/DL/EL/FL1-70[»]
5C3EX-ray3.70L1-70[»]
5C44X-ray3.95L1-70[»]
5C4AX-ray4.20L1-70[»]
5C4JX-ray4.00L1-70[»]
5C4XX-ray4.00L1-70[»]
5FJ8electron microscopy3.90L1-70[»]
5FJ9electron microscopy4.60L1-70[»]
5FJAelectron microscopy4.65L1-70[»]
5FMFelectron microscopy6.00L25-70[»]
5FYWelectron microscopy4.35L1-70[»]
5FZ5electron microscopy8.80L1-70[»]
5G5Lelectron microscopy4.80L1-70[»]
5IP7X-ray3.52L25-70[»]
5IP9X-ray3.90L25-70[»]
5LMXelectron microscopy4.90L1-70[»]
5M3Felectron microscopy3.80L1-70[»]
5M3Melectron microscopy4.00L1-70[»]
5M5Welectron microscopy3.80L1-70[»]
5M5Xelectron microscopy4.00L1-70[»]
5M5Yelectron microscopy4.00L1-70[»]
5M64electron microscopy4.60L1-70[»]
5N5Yelectron microscopy7.70L1-70[»]
5N5Zelectron microscopy7.70L1-70[»]
5N60electron microscopy7.70L1-70[»]
5N61electron microscopy3.40L1-70[»]
5OA1electron microscopy4.40L1-70[»]
5OQJelectron microscopy4.70L1-70[»]
5OQMelectron microscopy5.80L1-70[»]
5OT2X-ray3.20L1-70[»]
5SVAelectron microscopy15.30L1-70[»]
5U5QX-ray3.80L1-70[»]
5VVRelectron microscopy5.80L1-70[»]
5VVSelectron microscopy6.40L1-70[»]
5W4UX-ray3.60L1-70[»]
5W51X-ray3.40L1-70[»]
5W5Yelectron microscopy3.80L1-70[»]
5W64electron microscopy4.20L1-70[»]
5W65electron microscopy4.30L1-70[»]
5W66electron microscopy3.90L1-70[»]
6BLOX-ray3.40L1-70[»]
6BLPX-ray3.20L1-70[»]
6BM2X-ray3.40L1-70[»]
6BM4X-ray2.95L1-70[»]
6BQFX-ray3.35L1-70[»]
6CNBelectron microscopy4.10L1-70[»]
6CNCelectron microscopy4.10L1-70[»]
6CNDelectron microscopy4.80L1-70[»]
6CNFelectron microscopy4.50L1-70[»]
6EU0electron microscopy4.00L1-70[»]
6EU1electron microscopy3.40L1-70[»]
6EU2electron microscopy3.40L1-70[»]
6EU3electron microscopy3.30L1-70[»]
6F40electron microscopy3.70L1-70[»]
6F41electron microscopy4.30L1-70[»]
6F42electron microscopy5.50L1-70[»]
6F44electron microscopy4.20L1-70[»]
6GYKelectron microscopy5.10L1-70[»]
6GYLelectron microscopy4.80L1-70[»]
6GYMelectron microscopy6.70L1-70[»]
6H67electron microscopy3.60L1-70[»]
6H68electron microscopy4.60L1-70[»]
6HKOelectron microscopy3.42L1-70[»]
6HLQelectron microscopy3.18L1-70[»]
6HLRelectron microscopy3.18L1-70[»]
6HLSelectron microscopy3.21L1-70[»]
6I84electron microscopy4.40L1-70[»]
SMRiP40422
ModBaseiSearch...

Protein-protein interaction databases

BioGridi36577, 72 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-936N
IntActiP40422, 15 interactors
MINTiP40422
STRINGi4932.YHR143W-A

PTM databases

iPTMnetiP40422

Proteomic databases

MaxQBiP40422
PaxDbiP40422
PRIDEiP40422

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR143W-A_mRNA; YHR143W-A_mRNA; YHR143W-A
GeneIDi856547
KEGGisce:YHR143W-A

Organism-specific databases

EuPathDBiFungiDB:YHR143W-A
SGDiS000001185 RPC10

Phylogenomic databases

GeneTreeiENSGT00940000169869
HOGENOMiHOG000191755
InParanoidiP40422
KOiK03009
OMAiKYICAEC

Enzyme and pathway databases

BioCyciYEAST:G3O-31179-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

EvolutionaryTraceiP40422

Protein Ontology

More...
PROi
PR:P40422

Family and domain databases

DisProtiDP00818
InterProiView protein in InterPro
IPR006591 RNAP_P/RPABC4
IPR039747 RPABC4
IPR029040 RPABC4/Spt4
PANTHERiPTHR12056 PTHR12056, 1 hit
PfamiView protein in Pfam
PF03604 DNA_RNApol_7kD, 1 hit
SMARTiView protein in SMART
SM00659 RPOLCX, 1 hit
SUPFAMiSSF63393 SSF63393, 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 nameiRPAB4_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: P40422
Secondary accession number(s): D3DL93
<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, 1995
Last sequence update: February 1, 1995
Last modified: July 31, 2019
This is version 191 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, Direct protein sequencing, 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
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