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Protein

DNA-directed RNA polymerase II subunit RPB4

Gene

RPB4

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 polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB4 is part of a subcomplex with RPB7 that binds to a pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7 in the closed conformation thus preventing double-stranded DNA to enter the active site cleft. The RPB4-RPB7 subcomplex binds single-stranded DNA and RNA. The RPB4-RPB7 subcomplex is necessary for promoter-directed transcription initiation but is not required for recruitment of Pol II to active preinitiation complexes and seems to be dispensable for transcription elongation and termination. The RPB4-RPB7 subcomplex recruits FCP1 to Pol II. Involved in DNA repair of damage in the transcribed strand. RPB4 is dispensable under optimal growth conditions, but becomes essential during heat or cold shock and under nutrient depletion. Suppresses the RBP9-mediated transcription-coupled repair (TCR) subpathway of nucleotide excision repair (NER) but facilitates the RAD26-mediated TCR subpathway. Under stress conditions only, involved in mRNA export to the cytoplasm. Involved in mRNA decay. Promotes or enhances the deadenylation process of specific mRNAs and may recruit PAT1 and the LSM1-7 complex to these mRNAs, thus stimulating their decapping and further decay.7 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

Biological processmRNA processing, Transcription

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-31585-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-72165 mRNA Splicing - Minor Pathway
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 polymerase II subunit RPB4
Short name:
RNA polymerase II subunit B4
Alternative name(s):
B32
DNA-directed RNA polymerase II 32 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:RPB4
Ordered Locus Names:YJL140W
ORF Names:J0654
<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 X

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000003676 RPB4

<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_00000739841 – 221DNA-directed RNA polymerase II subunit RPB4Add BLAST221

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 residuei1N-acetylmethionineCombined sources1
Modified residuei91PhosphothreonineCombined sources1
Modified residuei92PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P20433

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

More...
PaxDbi
P20433

PRoteomics IDEntifications database

More...
PRIDEi
P20433

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P20433

<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 II (Pol II) complex consisting of 12 subunits. RPB4 and RPB7 form a dissociable subcomplex associated with the 10-subunit Pol II core complex. In exponentially proliferating cells, only approximately 20 % of the Pol II complexes contain the RPB4-RPB7 subcomplex. In starving cells, that enter stationary phase, RPB4-RPB7 is associated with Pol II in a stoechiometric manner. The RPB4-RPB7 subcomplex probably associates with TFG1. Interacts with LSM2 and PAT1.4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
33617, 143 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1891 RPB4-RPB7 subcomplex

Database of interacting proteins

More...
DIPi
DIP-55N

Protein interaction database and analysis system

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IntActi
P20433, 26 interactors

Molecular INTeraction database

More...
MINTi
P20433

STRING: functional protein association networks

More...
STRINGi
4932.YJL140W

<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

1221
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P20433

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

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SMRi
P20433

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
P20433

<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

Ensembl GeneTree

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GeneTreei
ENSGT00390000004912

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000195281

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P20433

KEGG Orthology (KO)

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KOi
K03012

Identification of Orthologs from Complete Genome Data

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OMAi
GTLECED

Database of Orthologous Groups

More...
OrthoDBi
EOG092C5NLC

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.1250.40, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR010997 HRDC-like_sf
IPR006590 RNA_pol_Rpb4/RPC9_core
IPR005574 RPB4/RPC9
IPR038324 Rpb4/RPC9_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03874 RNA_pol_Rpb4, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00657 RPOL4c, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47819 SSF47819, 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.

P20433-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNVSTSTFQT RRRRLKKVEE EENAATLQLG QEFQLKQINH QGEEEELIAL
60 70 80 90 100
NLSEARLVIK EALVERRRAF KRSQKKHKKK HLKHENANDE TTAVEDEDDD
110 120 130 140 150
LDEDDVNADD DDFMHSETRE KELESIDVLL EQTTGGNNKD LKNTMQYLTN
160 170 180 190 200
FSRFRDQETV GAVIQLLKST GLHPFEVAQL GSLACDTADE AKTLIPSLNN
210 220
KISDDELERI LKELSNLETL Y
Length:221
Mass (Da):25,414
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:i72A8A26871B87775
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
M27253 Genomic DNA Translation: AAA34996.1
X58099 Genomic DNA Translation: CAA41112.1
X87371 Genomic DNA Translation: CAA60815.1
Z49415 Genomic DNA Translation: CAA89435.1
AY557856 Genomic DNA Translation: AAS56182.1
BK006943 Genomic DNA Translation: DAA08660.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A32490

NCBI Reference Sequences

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RefSeqi
NP_012395.1, NM_001181573.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YJL140W_mRNA; YJL140W_mRNA; YJL140W

Database of genes from NCBI RefSeq genomes

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GeneIDi
853301

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YJL140W

<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
M27253 Genomic DNA Translation: AAA34996.1
X58099 Genomic DNA Translation: CAA41112.1
X87371 Genomic DNA Translation: CAA60815.1
Z49415 Genomic DNA Translation: CAA89435.1
AY557856 Genomic DNA Translation: AAS56182.1
BK006943 Genomic DNA Translation: DAA08660.1
PIRiA32490
RefSeqiNP_012395.1, NM_001181573.1

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
1NT9X-ray4.20D1-221[»]
1PQVX-ray3.80D1-85[»]
D115-221[»]
1WCMX-ray3.80D4-221[»]
1Y14X-ray2.30A/C35-221[»]
1Y1VX-ray3.80D1-221[»]
1Y1WX-ray4.00D1-221[»]
1Y1YX-ray4.00D1-221[»]
1Y77X-ray4.50D1-221[»]
2B63X-ray3.80D1-221[»]
2B8KX-ray4.15D1-221[»]
2JA5X-ray3.80D1-221[»]
2JA6X-ray4.00D1-221[»]
2JA7X-ray3.80D/P1-221[»]
2JA8X-ray3.80D1-221[»]
2R7ZX-ray3.80D1-221[»]
2R92X-ray3.80D1-221[»]
2R93X-ray4.00D1-221[»]
2VUMX-ray3.40D1-221[»]
3FKIX-ray3.88D1-221[»]
3H3VX-ray4.00E1-221[»]
3HOUX-ray3.20D/P1-221[»]
3HOVX-ray3.50D1-221[»]
3HOWX-ray3.60D1-221[»]
3HOXX-ray3.65D1-221[»]
3HOYX-ray3.40D1-221[»]
3HOZX-ray3.65D1-221[»]
3I4MX-ray3.70D1-221[»]
3I4NX-ray3.90D1-221[»]
3J0Kelectron microscopy36.00D1-221[»]
3J1Nelectron microscopy16.00D4-221[»]
3K1FX-ray4.30D1-221[»]
3PO2X-ray3.30D1-221[»]
3PO3X-ray3.30D1-221[»]
3QT1X-ray4.30D3-221[»]
4A3BX-ray3.50D1-221[»]
4A3CX-ray3.50D1-221[»]
4A3DX-ray3.40D1-221[»]
4A3EX-ray3.40D1-221[»]
4A3FX-ray3.50D1-221[»]
4A3GX-ray3.50D1-221[»]
4A3IX-ray3.80D1-221[»]
4A3JX-ray3.70D1-221[»]
4A3KX-ray3.50D1-221[»]
4A3LX-ray3.50D1-221[»]
4A3MX-ray3.90D1-221[»]
4A93X-ray3.40D1-221[»]
4BBRX-ray3.40D1-221[»]
4BBSX-ray3.60D1-221[»]
4BXXX-ray3.28D1-221[»]
4BXZX-ray4.80D1-221[»]
4BY1X-ray3.60D1-221[»]
4BY7X-ray3.15D1-221[»]
4V1Nelectron microscopy7.80D1-221[»]
4V1Oelectron microscopy9.70D1-221[»]
5C3EX-ray3.70D1-221[»]
5C44X-ray3.95D1-221[»]
5C4AX-ray4.20D1-221[»]
5C4XX-ray4.00D1-221[»]
5FMFelectron microscopy6.00D3-221[»]
5FYWelectron microscopy4.35D1-221[»]
5FZ5electron microscopy8.80D1-221[»]
5IP7X-ray3.52D1-221[»]
5IP9X-ray3.90D1-221[»]
5OQJelectron microscopy4.70D1-221[»]
5OQMelectron microscopy5.80D1-221[»]
5OT2X-ray3.20D1-221[»]
5SVAelectron microscopy15.30D1-221[»]
5U5QX-ray3.80D1-221[»]
5VVRelectron microscopy5.80D1-221[»]
5VVSelectron microscopy6.40D1-221[»]
ProteinModelPortaliP20433
SMRiP20433
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33617, 143 interactors
ComplexPortaliCPX-1891 RPB4-RPB7 subcomplex
DIPiDIP-55N
IntActiP20433, 26 interactors
MINTiP20433
STRINGi4932.YJL140W

PTM databases

iPTMnetiP20433

Proteomic databases

MaxQBiP20433
PaxDbiP20433
PRIDEiP20433

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL140W_mRNA; YJL140W_mRNA; YJL140W
GeneIDi853301
KEGGisce:YJL140W

Organism-specific databases

SGDiS000003676 RPB4

Phylogenomic databases

GeneTreeiENSGT00390000004912
HOGENOMiHOG000195281
InParanoidiP20433
KOiK03012
OMAiGTLECED
OrthoDBiEOG092C5NLC

Enzyme and pathway databases

BioCyciYEAST:G3O-31585-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-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

EvolutionaryTraceiP20433

Protein Ontology

More...
PROi
PR:P20433

Family and domain databases

Gene3Di1.20.1250.40, 2 hits
InterProiView protein in InterPro
IPR010997 HRDC-like_sf
IPR006590 RNA_pol_Rpb4/RPC9_core
IPR005574 RPB4/RPC9
IPR038324 Rpb4/RPC9_sf
PfamiView protein in Pfam
PF03874 RNA_pol_Rpb4, 1 hit
SMARTiView protein in SMART
SM00657 RPOL4c, 1 hit
SUPFAMiSSF47819 SSF47819, 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 nameiRPB4_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: P20433
Secondary accession number(s): D6VW44
<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 186 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 X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names
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