Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 199 (08 May 2019)
Sequence version 2 (01 Feb 1995)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

DNA-directed RNA polymerase II subunit RPB3

Gene

RPB3

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. RPB3 is part of the core element with the central large cleft and the clamp element that moves to open and close the cleft. Seems to be involved in transcription termination.1 Publication

Miscellaneous

Present with 10000 molecules/cell in log phase SD medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi86Zinc1
Metal bindingi88Zinc1
Metal bindingi92Zinc1
Metal bindingi95Zinc1

<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 processTranscription
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-31296-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-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-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 RPB3
Short name:
RNA polymerase II subunit 3
Short name:
RNA polymerase II subunit B3
Alternative name(s):
B44.5
DNA-directed RNA polymerase II 45 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:RPB3
Ordered Locus Names:YIL021W
<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 IX

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YIL021W

Saccharomyces Genome Database

More...
SGDi
S000001283 RPB3

<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 provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi9K → E: Transcript termination readthrough. 1 Publication1

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00001327482 – 318DNA-directed RNA polymerase II subunit RPB3Add BLAST317

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 residuei2N-acetylserineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P16370

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

More...
PaxDbi
P16370

PRoteomics IDEntifications database

More...
PRIDEi
P16370

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P16370

<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.3 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
34967, 611 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2662 DNA-directed RNA polymerase II complex

Database of interacting proteins

More...
DIPi
DIP-837N

Protein interaction database and analysis system

More...
IntActi
P16370, 41 interactors

Molecular INTeraction database

More...
MINTi
P16370

STRING: functional protein association networks

More...
STRINGi
4932.YIL021W

<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

1318
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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-ray3.10C1-318[»]
1I50X-ray2.80C1-318[»]
1I6HX-ray3.30C1-318[»]
1K83X-ray2.80C1-318[»]
1NIKX-ray4.10C1-318[»]
1NT9X-ray4.20C1-318[»]
1PQVX-ray3.80C1-318[»]
1R5UX-ray4.50C1-318[»]
1R9SX-ray4.25C1-318[»]
1R9TX-ray3.50C1-318[»]
1SFOX-ray3.61C1-318[»]
1TWAX-ray3.20C1-318[»]
1TWCX-ray3.00C1-318[»]
1TWFX-ray2.30C1-318[»]
1TWGX-ray3.30C1-318[»]
1TWHX-ray3.40C1-318[»]
1WCMX-ray3.80C1-318[»]
1Y1VX-ray3.80C1-318[»]
1Y1WX-ray4.00C1-318[»]
1Y1YX-ray4.00C1-318[»]
1Y77X-ray4.50C1-318[»]
2B63X-ray3.80C1-318[»]
2B8KX-ray4.15C1-318[»]
2E2HX-ray3.95C1-318[»]
2E2IX-ray3.41C1-318[»]
2E2JX-ray3.50C1-318[»]
2JA5X-ray3.80C1-318[»]
2JA6X-ray4.00C1-318[»]
2JA7X-ray3.80C/O1-318[»]
2JA8X-ray3.80C1-318[»]
2NVQX-ray2.90C1-318[»]
2NVTX-ray3.36C1-318[»]
2NVXX-ray3.60C1-318[»]
2NVYX-ray3.40C1-318[»]
2NVZX-ray4.30C1-318[»]
2R7ZX-ray3.80C1-318[»]
2R92X-ray3.80C1-318[»]
2R93X-ray4.00C1-318[»]
2VUMX-ray3.40C1-318[»]
2YU9X-ray3.40C1-318[»]
3CQZX-ray2.80C1-318[»]
3FKIX-ray3.88C1-318[»]
3GTGX-ray3.78C1-318[»]
3GTJX-ray3.42C1-318[»]
3GTKX-ray3.80C1-318[»]
3GTLX-ray3.38C1-318[»]
3GTMX-ray3.80C1-318[»]
3GTOX-ray4.00C1-318[»]
3GTPX-ray3.90C1-318[»]
3GTQX-ray3.80C1-318[»]
3H3VX-ray4.00D1-318[»]
3HOUX-ray3.20C/O1-318[»]
3HOVX-ray3.50C1-318[»]
3HOWX-ray3.60C2-318[»]
3HOXX-ray3.65C2-318[»]
3HOYX-ray3.40C2-318[»]
3HOZX-ray3.65C2-318[»]
3I4MX-ray3.70C1-318[»]
3I4NX-ray3.90C1-318[»]
3J0Kelectron microscopy36.00C1-268[»]
3J1Nelectron microscopy16.00C1-268[»]
3K1FX-ray4.30C1-318[»]
3K7AX-ray3.80C1-318[»]
3M3YX-ray3.18C1-318[»]
3M4OX-ray3.57C1-318[»]
3PO2X-ray3.30C1-318[»]
3PO3X-ray3.30C1-318[»]
3QT1X-ray4.30C1-318[»]
3RZDX-ray3.30C1-318[»]
3RZOX-ray3.00C1-318[»]
3S14X-ray2.85C1-318[»]
3S15X-ray3.30C1-318[»]
3S16X-ray3.24C1-318[»]
3S17X-ray3.20C1-318[»]
3S1MX-ray3.13C1-318[»]
3S1NX-ray3.10C1-318[»]
3S1QX-ray3.30C1-318[»]
3S1RX-ray3.20C1-318[»]
3S2DX-ray3.20C1-318[»]
3S2HX-ray3.30C1-318[»]
4A3BX-ray3.50C1-318[»]
4A3CX-ray3.50C1-318[»]
4A3DX-ray3.40C1-318[»]
4A3EX-ray3.40C1-318[»]
4A3FX-ray3.50C1-318[»]
4A3GX-ray3.50C1-318[»]
4A3IX-ray3.80C1-318[»]
4A3JX-ray3.70C1-318[»]
4A3KX-ray3.50C1-318[»]
4A3LX-ray3.50C1-318[»]
4A3MX-ray3.90C1-318[»]
4A93X-ray3.40C1-318[»]
4BBRX-ray3.40C1-318[»]
4BBSX-ray3.60C1-318[»]
4BXXX-ray3.28C1-318[»]
4BXZX-ray4.80C1-318[»]
4BY1X-ray3.60C1-318[»]
4BY7X-ray3.15C1-318[»]
4V1Melectron microscopy6.60C1-318[»]
4V1Nelectron microscopy7.80C1-318[»]
4V1Oelectron microscopy9.70C1-318[»]
4X67X-ray4.10C1-318[»]
4X6AX-ray3.96C1-318[»]
4Y52X-ray3.50C1-318[»]
4Y7NX-ray3.30C1-318[»]
5C3EX-ray3.70C1-318[»]
5C44X-ray3.95C1-318[»]
5C4AX-ray4.20C1-318[»]
5C4JX-ray4.00C1-318[»]
5C4XX-ray4.00C1-318[»]
5FMFelectron microscopy6.00C3-268[»]
5FYWelectron microscopy4.35C1-318[»]
5FZ5electron microscopy8.80C1-318[»]
5IP7X-ray3.52C3-268[»]
5IP9X-ray3.90C3-268[»]
5OQJelectron microscopy4.70C1-318[»]
5OQMelectron microscopy5.80C1-318[»]
5OT2X-ray3.20C1-318[»]
5SVAelectron microscopy15.30C1-318[»]
5U5QX-ray3.80C1-318[»]
5VVRelectron microscopy5.80C1-318[»]
5VVSelectron microscopy6.40C1-318[»]
5W4UX-ray3.60C1-318[»]
5W51X-ray3.40C1-318[»]
6BLOX-ray3.40C1-318[»]
6BLPX-ray3.20C1-318[»]
6BM2X-ray3.40C1-318[»]
6BM4X-ray2.95C1-318[»]
6BQFX-ray3.35C1-318[»]
6GYKelectron microscopy5.10C1-318[»]
6GYLelectron microscopy4.80C1-318[»]
6GYMelectron microscopy6.70C1-318[»]
6I84electron microscopy4.40C1-318[»]

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

More...
SMRi
P16370

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P16370

<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

More...
GeneTreei
ENSGT00950000183100

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000230844

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P16370

KEGG Orthology (KO)

More...
KOi
K03011

Identification of Orthologs from Complete Genome Data

More...
OMAi
PENIVMM

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.170.120.12, 1 hit
3.30.1360.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001514 DNA-dir_RNA_pol_30-40kDasu_CS
IPR011262 DNA-dir_RNA_pol_insert
IPR011263 DNA-dir_RNA_pol_RpoA/D/Rpb3
IPR036603 RBP11-like
IPR036643 RNApol_insert_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01000 RNA_pol_A_bac, 1 hit
PF01193 RNA_pol_L, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00662 RPOLD, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF55257 SSF55257, 1 hit
SSF56553 SSF56553, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00446 RNA_POL_D_30KD, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P16370-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSEEGPQVKI REASKDNVDF ILSNVDLAMA NSLRRVMIAE IPTLAIDSVE
60 70 80 90 100
VETNTTVLAD EFIAHRLGLI PLQSMDIEQL EYSRDCFCED HCDKCSVVLT
110 120 130 140 150
LQAFGESEST TNVYSKDLVI VSNLMGRNIG HPIIQDKEGN GVLICKLRKG
160 170 180 190 200
QELKLTCVAK KGIAKEHAKW GPAAAIEFEY DPWNKLKHTD YWYEQDSAKE
210 220 230 240 250
WPQSKNCEYE DPPNEGDPFD YKAQADTFYM NVESVGSIPV DQVVVRGIDT
260 270 280 290 300
LQKKVASILL ALTQMDQDKV NFASGDNNTA SNMLGSNEDV MMTGAEQDPY
310
SNASQMGNTG SGGYDNAW
Length:318
Mass (Da):35,298
Last modified:February 1, 1995 - 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:i8E1D1E6BB7B51D89
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti175A → G in AAA34889 (PubMed:2685562).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti30A → D in mutant RPB3-1. 1

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
Z46881 Genomic DNA Translation: CAA86971.1
M27496 Genomic DNA Translation: AAA34889.1
BK006942 Genomic DNA Translation: DAA08524.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S49961

NCBI Reference Sequences

More...
RefSeqi
NP_012243.3, NM_001179371.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YIL021W_mRNA; YIL021W_mRNA; YIL021W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
854791

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YIL021W

Keywords - Coding sequence diversityi

Polymorphism

<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
Z46881 Genomic DNA Translation: CAA86971.1
M27496 Genomic DNA Translation: AAA34889.1
BK006942 Genomic DNA Translation: DAA08524.1
PIRiS49961
RefSeqiNP_012243.3, NM_001179371.3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I3QX-ray3.10C1-318[»]
1I50X-ray2.80C1-318[»]
1I6HX-ray3.30C1-318[»]
1K83X-ray2.80C1-318[»]
1NIKX-ray4.10C1-318[»]
1NT9X-ray4.20C1-318[»]
1PQVX-ray3.80C1-318[»]
1R5UX-ray4.50C1-318[»]
1R9SX-ray4.25C1-318[»]
1R9TX-ray3.50C1-318[»]
1SFOX-ray3.61C1-318[»]
1TWAX-ray3.20C1-318[»]
1TWCX-ray3.00C1-318[»]
1TWFX-ray2.30C1-318[»]
1TWGX-ray3.30C1-318[»]
1TWHX-ray3.40C1-318[»]
1WCMX-ray3.80C1-318[»]
1Y1VX-ray3.80C1-318[»]
1Y1WX-ray4.00C1-318[»]
1Y1YX-ray4.00C1-318[»]
1Y77X-ray4.50C1-318[»]
2B63X-ray3.80C1-318[»]
2B8KX-ray4.15C1-318[»]
2E2HX-ray3.95C1-318[»]
2E2IX-ray3.41C1-318[»]
2E2JX-ray3.50C1-318[»]
2JA5X-ray3.80C1-318[»]
2JA6X-ray4.00C1-318[»]
2JA7X-ray3.80C/O1-318[»]
2JA8X-ray3.80C1-318[»]
2NVQX-ray2.90C1-318[»]
2NVTX-ray3.36C1-318[»]
2NVXX-ray3.60C1-318[»]
2NVYX-ray3.40C1-318[»]
2NVZX-ray4.30C1-318[»]
2R7ZX-ray3.80C1-318[»]
2R92X-ray3.80C1-318[»]
2R93X-ray4.00C1-318[»]
2VUMX-ray3.40C1-318[»]
2YU9X-ray3.40C1-318[»]
3CQZX-ray2.80C1-318[»]
3FKIX-ray3.88C1-318[»]
3GTGX-ray3.78C1-318[»]
3GTJX-ray3.42C1-318[»]
3GTKX-ray3.80C1-318[»]
3GTLX-ray3.38C1-318[»]
3GTMX-ray3.80C1-318[»]
3GTOX-ray4.00C1-318[»]
3GTPX-ray3.90C1-318[»]
3GTQX-ray3.80C1-318[»]
3H3VX-ray4.00D1-318[»]
3HOUX-ray3.20C/O1-318[»]
3HOVX-ray3.50C1-318[»]
3HOWX-ray3.60C2-318[»]
3HOXX-ray3.65C2-318[»]
3HOYX-ray3.40C2-318[»]
3HOZX-ray3.65C2-318[»]
3I4MX-ray3.70C1-318[»]
3I4NX-ray3.90C1-318[»]
3J0Kelectron microscopy36.00C1-268[»]
3J1Nelectron microscopy16.00C1-268[»]
3K1FX-ray4.30C1-318[»]
3K7AX-ray3.80C1-318[»]
3M3YX-ray3.18C1-318[»]
3M4OX-ray3.57C1-318[»]
3PO2X-ray3.30C1-318[»]
3PO3X-ray3.30C1-318[»]
3QT1X-ray4.30C1-318[»]
3RZDX-ray3.30C1-318[»]
3RZOX-ray3.00C1-318[»]
3S14X-ray2.85C1-318[»]
3S15X-ray3.30C1-318[»]
3S16X-ray3.24C1-318[»]
3S17X-ray3.20C1-318[»]
3S1MX-ray3.13C1-318[»]
3S1NX-ray3.10C1-318[»]
3S1QX-ray3.30C1-318[»]
3S1RX-ray3.20C1-318[»]
3S2DX-ray3.20C1-318[»]
3S2HX-ray3.30C1-318[»]
4A3BX-ray3.50C1-318[»]
4A3CX-ray3.50C1-318[»]
4A3DX-ray3.40C1-318[»]
4A3EX-ray3.40C1-318[»]
4A3FX-ray3.50C1-318[»]
4A3GX-ray3.50C1-318[»]
4A3IX-ray3.80C1-318[»]
4A3JX-ray3.70C1-318[»]
4A3KX-ray3.50C1-318[»]
4A3LX-ray3.50C1-318[»]
4A3MX-ray3.90C1-318[»]
4A93X-ray3.40C1-318[»]
4BBRX-ray3.40C1-318[»]
4BBSX-ray3.60C1-318[»]
4BXXX-ray3.28C1-318[»]
4BXZX-ray4.80C1-318[»]
4BY1X-ray3.60C1-318[»]
4BY7X-ray3.15C1-318[»]
4V1Melectron microscopy6.60C1-318[»]
4V1Nelectron microscopy7.80C1-318[»]
4V1Oelectron microscopy9.70C1-318[»]
4X67X-ray4.10C1-318[»]
4X6AX-ray3.96C1-318[»]
4Y52X-ray3.50C1-318[»]
4Y7NX-ray3.30C1-318[»]
5C3EX-ray3.70C1-318[»]
5C44X-ray3.95C1-318[»]
5C4AX-ray4.20C1-318[»]
5C4JX-ray4.00C1-318[»]
5C4XX-ray4.00C1-318[»]
5FMFelectron microscopy6.00C3-268[»]
5FYWelectron microscopy4.35C1-318[»]
5FZ5electron microscopy8.80C1-318[»]
5IP7X-ray3.52C3-268[»]
5IP9X-ray3.90C3-268[»]
5OQJelectron microscopy4.70C1-318[»]
5OQMelectron microscopy5.80C1-318[»]
5OT2X-ray3.20C1-318[»]
5SVAelectron microscopy15.30C1-318[»]
5U5QX-ray3.80C1-318[»]
5VVRelectron microscopy5.80C1-318[»]
5VVSelectron microscopy6.40C1-318[»]
5W4UX-ray3.60C1-318[»]
5W51X-ray3.40C1-318[»]
6BLOX-ray3.40C1-318[»]
6BLPX-ray3.20C1-318[»]
6BM2X-ray3.40C1-318[»]
6BM4X-ray2.95C1-318[»]
6BQFX-ray3.35C1-318[»]
6GYKelectron microscopy5.10C1-318[»]
6GYLelectron microscopy4.80C1-318[»]
6GYMelectron microscopy6.70C1-318[»]
6I84electron microscopy4.40C1-318[»]
SMRiP16370
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34967, 611 interactors
ComplexPortaliCPX-2662 DNA-directed RNA polymerase II complex
DIPiDIP-837N
IntActiP16370, 41 interactors
MINTiP16370
STRINGi4932.YIL021W

PTM databases

iPTMnetiP16370

Proteomic databases

MaxQBiP16370
PaxDbiP16370
PRIDEiP16370

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL021W_mRNA; YIL021W_mRNA; YIL021W
GeneIDi854791
KEGGisce:YIL021W

Organism-specific databases

EuPathDBiFungiDB:YIL021W
SGDiS000001283 RPB3

Phylogenomic databases

GeneTreeiENSGT00950000183100
HOGENOMiHOG000230844
InParanoidiP16370
KOiK03011
OMAiPENIVMM

Enzyme and pathway databases

BioCyciYEAST:G3O-31296-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-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-77075 RNA Pol II CTD phosphorylation and interaction with CE
R-SCE-9018519 Estrogen-dependent gene expression

Miscellaneous databases

EvolutionaryTraceiP16370

Protein Ontology

More...
PROi
PR:P16370

Family and domain databases

Gene3Di2.170.120.12, 1 hit
3.30.1360.10, 1 hit
InterProiView protein in InterPro
IPR001514 DNA-dir_RNA_pol_30-40kDasu_CS
IPR011262 DNA-dir_RNA_pol_insert
IPR011263 DNA-dir_RNA_pol_RpoA/D/Rpb3
IPR036603 RBP11-like
IPR036643 RNApol_insert_sf
PfamiView protein in Pfam
PF01000 RNA_pol_A_bac, 1 hit
PF01193 RNA_pol_L, 1 hit
SMARTiView protein in SMART
SM00662 RPOLD, 1 hit
SUPFAMiSSF55257 SSF55257, 1 hit
SSF56553 SSF56553, 1 hit
PROSITEiView protein in PROSITE
PS00446 RNA_POL_D_30KD, 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 nameiRPB3_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: P16370
Secondary accession number(s): D6VVQ8
<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, 1990
Last sequence update: February 1, 1995
Last modified: May 8, 2019
This is version 199 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, Complete proteome, Direct protein sequencing, 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 IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again