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UniProtKB - P19388 (RPAB1_HUMAN)

Entry version 217 (29 Sep 2021)
Sequence version 4 (17 Oct 2006)
Previous versions | rss
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Protein

DNA-directed RNA polymerases I, II, and III subunit RPABC1

Gene

POLR2E

Organism
Homo sapiens (Human)
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. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2E/RPB5 is part of the lower jaw surrounding the central large cleft and thought to grab the incoming DNA template. Seems to be the major component in this process (By similarity).

By similarity1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • DNA binding Source: InterPro
  • DNA-directed 5'-3' RNA polymerase activity Source: ProtInc
Complete GO annotation on QuickGO ...

GO - Biological processi

  • transcription by RNA polymerase II Source: UniProtKB
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 processHost-virus interaction, Transcription

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P19388

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-112382, Formation of RNA Pol II elongation complex
R-HSA-113418, Formation of the Early Elongation Complex
R-HSA-167152, Formation of HIV elongation complex in the absence of HIV Tat
R-HSA-167158, Formation of the HIV-1 Early Elongation Complex
R-HSA-167160, RNA Pol II CTD phosphorylation and interaction with CE during HIV infection
R-HSA-167161, HIV Transcription Initiation
R-HSA-167162, RNA Polymerase II HIV Promoter Escape
R-HSA-167172, Transcription of the HIV genome
R-HSA-167200, Formation of HIV-1 elongation complex containing HIV-1 Tat
R-HSA-167238, Pausing and recovery of Tat-mediated HIV elongation
R-HSA-167242, Abortive elongation of HIV-1 transcript in the absence of Tat
R-HSA-167243, Tat-mediated HIV elongation arrest and recovery
R-HSA-167246, Tat-mediated elongation of the HIV-1 transcript
R-HSA-167287, HIV elongation arrest and recovery
R-HSA-167290, Pausing and recovery of HIV elongation
R-HSA-168325, Viral Messenger RNA Synthesis
R-HSA-1834949, Cytosolic sensors of pathogen-associated DNA
R-HSA-203927, MicroRNA (miRNA) biogenesis
R-HSA-427413, NoRC negatively regulates rRNA expression
R-HSA-5250924, B-WICH complex positively regulates rRNA expression
R-HSA-5578749, Transcriptional regulation by small RNAs
R-HSA-5601884, PIWI-interacting RNA (piRNA) biogenesis
R-HSA-5617472, Activation of anterior HOX genes in hindbrain development during early embryogenesis
R-HSA-674695, RNA Polymerase II Pre-transcription Events
R-HSA-6781823, Formation of TC-NER Pre-Incision Complex
R-HSA-6781827, Transcription-Coupled Nucleotide Excision Repair (TC-NER)
R-HSA-6782135, Dual incision in TC-NER
R-HSA-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-HSA-6796648, TP53 Regulates Transcription of DNA Repair Genes
R-HSA-6803529, FGFR2 alternative splicing
R-HSA-6807505, RNA polymerase II transcribes snRNA genes
R-HSA-72086, mRNA Capping
R-HSA-72163, mRNA Splicing - Major Pathway
R-HSA-72165, mRNA Splicing - Minor Pathway
R-HSA-72203, Processing of Capped Intron-Containing Pre-mRNA
R-HSA-73762, RNA Polymerase I Transcription Initiation
R-HSA-73772, RNA Polymerase I Promoter Escape
R-HSA-73776, RNA Polymerase II Promoter Escape
R-HSA-73779, RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
R-HSA-73780, RNA Polymerase III Chain Elongation
R-HSA-73863, RNA Polymerase I Transcription Termination
R-HSA-73980, RNA Polymerase III Transcription Termination
R-HSA-749476, RNA Polymerase III Abortive And Retractive Initiation
R-HSA-75953, RNA Polymerase II Transcription Initiation
R-HSA-75955, RNA Polymerase II Transcription Elongation
R-HSA-76042, RNA Polymerase II Transcription Initiation And Promoter Clearance
R-HSA-76061, RNA Polymerase III Transcription Initiation From Type 1 Promoter
R-HSA-76066, RNA Polymerase III Transcription Initiation From Type 2 Promoter
R-HSA-76071, RNA Polymerase III Transcription Initiation From Type 3 Promoter
R-HSA-77075, RNA Pol II CTD phosphorylation and interaction with CE
R-HSA-8851708, Signaling by FGFR2 IIIa TM
R-HSA-9018519, Estrogen-dependent gene expression
R-HSA-9670095, Inhibition of DNA recombination at telomere

SIGNOR Signaling Network Open Resource

More...SIGNORi		P19388

<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 RPABC1
Short name:
RNA polymerases I, II, and III subunit ABC1
Alternative name(s):
DNA-directed RNA polymerase II 23 kDa polypeptide
DNA-directed RNA polymerase II subunit E
RPB5 homolog
XAP4
<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:POLR2E
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <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 19

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:9192, POLR2E

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		180664, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P19388

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000099817

<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 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

Organism-specific databases

DisGeNET

More...DisGeNETi		5434

Open Targets

More...OpenTargetsi		ENSG00000099817

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33512

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P19388, Tbio

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		POLR2E

Domain mapping of disease mutations (DMDM)

More...DMDMi		116242767

<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_00001460751 – 210DNA-directed RNA polymerases I, II, and III subunit RPABC1Add BLAST210

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
<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-linki81Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P19388

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P19388

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P19388

MaxQB - The MaxQuant DataBase

More...MaxQBi		P19388

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

More...PaxDbi		P19388

PeptideAtlas

More...PeptideAtlasi		P19388

PRoteomics IDEntifications database

More...PRIDEi		P19388

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		53653

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P19388

2D gel databases

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		IPI00291093

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P19388

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P19388, 1 site, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P19388

MetOSite database of methionine sulfoxide sites

More...MetOSitei		P19388

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P19388

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000099817, Expressed in heart left ventricle and 252 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P19388, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P19388, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000099817, Low tissue specificity

<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 consisting of at least 13, 12 and 17 subunits, respectively (PubMed:9852112, PubMed:16809778). In RNA Pol II, this subunit is present in 2-fold molar excess over the other subunits (PubMed:9852112).

Component of the PAQosome complex which is responsible for the biogenesis of several protein complexes and which consists of R2TP complex members RUVBL1, RUVBL2, RPAP3 and PIH1D1, URI complex members PFDN2, PFDN6, PDRG1, UXT and URI1 as well as ASDURF, POLR2E and DNAAF10/WDR92 (PubMed:31738558).

Interacts with URI1 (PubMed:9819440).

4 Publications

(Microbial infection) Interacts with HBV protein X.

1 Publication

<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

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		111430, 198 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-6145, PAQosome co-chaperone complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P19388

Database of interacting proteins

More...DIPi		DIP-56N

Protein interaction database and analysis system

More...IntActi		P19388, 150 interactors

Molecular INTeraction database

More...MINTi		P19388

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000478303

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P19388, 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

1210
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		P19388

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<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 Rpo5/eukaryotic RPB5 RNA polymerase subunit family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3218, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00390000013841

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_058320_0_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P19388

Identification of Orthologs from Complete Genome Data

More...OMAi		VRDRGYF

Database of Orthologous Groups

More...OrthoDBi		1255823at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P19388

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.1340.10, 1 hit
3.90.940.20, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00025, RNApol_Rpo5_RPB5, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR014381, DNA_RNA_pol_RPB5_euk/virus
IPR005571, RNA_pol_Rpb5_N
IPR036710, RNA_pol_Rpb5_N_sf
IPR000783, RNA_pol_subH/Rpb5_C
IPR020608, RNA_pol_subH/Rpb5_CS
IPR039531, Rpb5-like
IPR035913, RPB5-like_sf
IPR020609, RpoH/RPB5

The PANTHER Classification System

More...PANTHERi		PTHR10535, PTHR10535, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01191, RNA_pol_Rpb5_C, 1 hit
PF03871, RNA_pol_Rpb5_N, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000747, RPB5, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53036, SSF53036, 1 hit
SSF55287, SSF55287, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS01110, RNA_POL_H_23KD, 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>Sequence (1+)i

<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.

This entry has 1 described isoform and 6 potential isoforms that are computationally mapped.Show allAlign All

P19388-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDDEEETYRL WKIRKTIMQL CHDRGYLVTQ DELDQTLEEF KAQSGDKPSE 
        60         70         80         90        100
GRPRRTDLTV LVAHNDDPTD QMFVFFPEEP KVGIKTIKVY CQRMQEENIT 
       110        120        130        140        150
RALIVVQQGM TPSAKQSLVD MAPKYILEQF LQQELLINIT EHELVPEHVV 
       160        170        180        190        200
MTKEEVTELL ARYKLRENQL PRIQAGDPVA RYFGIKRGQV VKIIRPSETA 
       210
GRYITYRLVQ
Length:210
Mass (Da):24,551
Last modified:October 17, 2006 - v4
<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:i1E88AFDBCF9C8535
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WVZ9A0A087WVZ9_HUMAN
DNA-directed RNA polymerase II subu...
POLR2E
184Annotation score:

Annotation score:2 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>
A0A0A0MQR7A0A0A0MQR7_HUMAN
DNA-directed RNA polymerase II subu...
POLR2E
204Annotation score:

Annotation score:2 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>
A0A087WWX0A0A087WWX0_HUMAN
DNA-directed RNA polymerases I, II,...
POLR2E
134Annotation score:

Annotation score:1 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>
A0A087WVN5A0A087WVN5_HUMAN
DNA-directed RNA polymerases I, II,...
POLR2E
83Annotation score:

Annotation score:1 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>
K7EJ87K7EJ87_HUMAN
DNA-directed RNA polymerases I, II,...
POLR2E
68Annotation score:

Annotation score:1 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>
K7EQN2K7EQN2_HUMAN
DNA-directed RNA polymerases I, II,...
POLR2E
51Annotation score:

Annotation score:1 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 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 conflicti132Q → E (PubMed:2753903).Curated1
Sequence conflicti132Q → E (PubMed:7828586).Curated1
Sequence conflicti157T → S in BAA07406 (PubMed:7828586).Curated1
Sequence conflicti185I → V in AAH34144 (PubMed:15489334).Curated1
Sequence conflicti186K → R in BAA07406 (PubMed:7828586).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 variantiVAR_02825944S → F5 PublicationsCorresponds to variant dbSNP:rs12459404Ensembl.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
J04965 mRNA Translation: AAA62401.1 Sequence problems.
S42643 mRNA Translation: AAB19339.1
D38251 mRNA Translation: BAA07406.1
AK312625 mRNA Translation: BAG35511.1
AC004151 Genomic DNA Translation: AAC03238.1
CH471139 Genomic DNA Translation: EAW69548.1
CH471139 Genomic DNA Translation: EAW69549.1
BC004441 mRNA Translation: AAH04441.1
BC034144 mRNA Translation: AAH34144.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS12056.1

Protein sequence database of the Protein Information Resource

More...PIRi		S52002, A32618

NCBI Reference Sequences

More...RefSeqi		NP_002686.2, NM_002695.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000586746; ENSP00000464739; ENSG00000099817
ENST00000612655; ENSP00000485021; ENSG00000099817
ENST00000615234; ENSP00000478303; ENSG00000099817

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5434

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5434

UCSC genome browser

More...UCSCi		uc002lre.5, human

<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
J04965 mRNA Translation: AAA62401.1 Sequence problems.
S42643 mRNA Translation: AAB19339.1
D38251 mRNA Translation: BAA07406.1
AK312625 mRNA Translation: BAG35511.1
AC004151 Genomic DNA Translation: AAC03238.1
CH471139 Genomic DNA Translation: EAW69548.1
CH471139 Genomic DNA Translation: EAW69549.1
BC004441 mRNA Translation: AAH04441.1
BC034144 mRNA Translation: AAH34144.1
CCDSiCCDS12056.1
PIRiS52002, A32618
RefSeqiNP_002686.2, NM_002695.3

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
5IY6electron microscopy7.20E1-210[»]
5IY7electron microscopy8.60E1-210[»]
5IY8electron microscopy7.90E1-210[»]
5IY9electron microscopy6.30E1-210[»]
5IYAelectron microscopy5.40E1-210[»]
5IYBelectron microscopy3.90E1-210[»]
5IYCelectron microscopy3.90E1-210[»]
5IYDelectron microscopy3.90E1-210[»]
6DRDelectron microscopy3.90E1-210[»]
6O9Lelectron microscopy7.20E1-210[»]
6XREelectron microscopy4.60E1-210[»]
7A6Helectron microscopy3.30E1-210[»]
7AE1electron microscopy2.80E1-210[»]
7AE3electron microscopy3.10E1-210[»]
7AEAelectron microscopy3.40E1-210[»]
7ASTelectron microscopy4.00F1-210[»]
7D58electron microscopy2.90E1-210[»]
7D59electron microscopy3.10E1-210[»]
7DN3electron microscopy3.50E1-210[»]
7DU2electron microscopy3.35E1-210[»]
7LBMelectron microscopy4.80E1-210[»]
SMRiP19388
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111430, 198 interactors
ComplexPortaliCPX-6145, PAQosome co-chaperone complex
CORUMiP19388
DIPiDIP-56N
IntActiP19388, 150 interactors
MINTiP19388
STRINGi9606.ENSP00000478303

PTM databases

GlyGeniP19388, 1 site, 1 O-linked glycan (1 site)
iPTMnetiP19388
MetOSiteiP19388
PhosphoSitePlusiP19388

Genetic variation databases

BioMutaiPOLR2E
DMDMi116242767

2D gel databases

REPRODUCTION-2DPAGEiIPI00291093
SWISS-2DPAGEiP19388

Proteomic databases

EPDiP19388
jPOSTiP19388
MassIVEiP19388
MaxQBiP19388
PaxDbiP19388
PeptideAtlasiP19388
PRIDEiP19388
ProteomicsDBi53653
TopDownProteomicsiP19388

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		22550, 309 antibodies

The DNASU plasmid repository

More...DNASUi		5434

Genome annotation databases

EnsembliENST00000586746; ENSP00000464739; ENSG00000099817
ENST00000612655; ENSP00000485021; ENSG00000099817
ENST00000615234; ENSP00000478303; ENSG00000099817
GeneIDi5434
KEGGihsa:5434
UCSCiuc002lre.5, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5434
DisGeNETi5434

GeneCards: human genes, protein and diseases

More...GeneCardsi		POLR2E
HGNCiHGNC:9192, POLR2E
HPAiENSG00000099817, Low tissue specificity
MIMi180664, gene
neXtProtiNX_P19388
OpenTargetsiENSG00000099817
PharmGKBiPA33512
VEuPathDBiHostDB:ENSG00000099817

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3218, Eukaryota
GeneTreeiENSGT00390000013841
HOGENOMiCLU_058320_0_1_1
InParanoidiP19388
OMAiVRDRGYF
OrthoDBi1255823at2759
PhylomeDBiP19388

Enzyme and pathway databases

PathwayCommonsiP19388
ReactomeiR-HSA-112382, Formation of RNA Pol II elongation complex
R-HSA-113418, Formation of the Early Elongation Complex
R-HSA-167152, Formation of HIV elongation complex in the absence of HIV Tat
R-HSA-167158, Formation of the HIV-1 Early Elongation Complex
R-HSA-167160, RNA Pol II CTD phosphorylation and interaction with CE during HIV infection
R-HSA-167161, HIV Transcription Initiation
R-HSA-167162, RNA Polymerase II HIV Promoter Escape
R-HSA-167172, Transcription of the HIV genome
R-HSA-167200, Formation of HIV-1 elongation complex containing HIV-1 Tat
R-HSA-167238, Pausing and recovery of Tat-mediated HIV elongation
R-HSA-167242, Abortive elongation of HIV-1 transcript in the absence of Tat
R-HSA-167243, Tat-mediated HIV elongation arrest and recovery
R-HSA-167246, Tat-mediated elongation of the HIV-1 transcript
R-HSA-167287, HIV elongation arrest and recovery
R-HSA-167290, Pausing and recovery of HIV elongation
R-HSA-168325, Viral Messenger RNA Synthesis
R-HSA-1834949, Cytosolic sensors of pathogen-associated DNA
R-HSA-203927, MicroRNA (miRNA) biogenesis
R-HSA-427413, NoRC negatively regulates rRNA expression
R-HSA-5250924, B-WICH complex positively regulates rRNA expression
R-HSA-5578749, Transcriptional regulation by small RNAs
R-HSA-5601884, PIWI-interacting RNA (piRNA) biogenesis
R-HSA-5617472, Activation of anterior HOX genes in hindbrain development during early embryogenesis
R-HSA-674695, RNA Polymerase II Pre-transcription Events
R-HSA-6781823, Formation of TC-NER Pre-Incision Complex
R-HSA-6781827, Transcription-Coupled Nucleotide Excision Repair (TC-NER)
R-HSA-6782135, Dual incision in TC-NER
R-HSA-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-HSA-6796648, TP53 Regulates Transcription of DNA Repair Genes
R-HSA-6803529, FGFR2 alternative splicing
R-HSA-6807505, RNA polymerase II transcribes snRNA genes
R-HSA-72086, mRNA Capping
R-HSA-72163, mRNA Splicing - Major Pathway
R-HSA-72165, mRNA Splicing - Minor Pathway
R-HSA-72203, Processing of Capped Intron-Containing Pre-mRNA
R-HSA-73762, RNA Polymerase I Transcription Initiation
R-HSA-73772, RNA Polymerase I Promoter Escape
R-HSA-73776, RNA Polymerase II Promoter Escape
R-HSA-73779, RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
R-HSA-73780, RNA Polymerase III Chain Elongation
R-HSA-73863, RNA Polymerase I Transcription Termination
R-HSA-73980, RNA Polymerase III Transcription Termination
R-HSA-749476, RNA Polymerase III Abortive And Retractive Initiation
R-HSA-75953, RNA Polymerase II Transcription Initiation
R-HSA-75955, RNA Polymerase II Transcription Elongation
R-HSA-76042, RNA Polymerase II Transcription Initiation And Promoter Clearance
R-HSA-76061, RNA Polymerase III Transcription Initiation From Type 1 Promoter
R-HSA-76066, RNA Polymerase III Transcription Initiation From Type 2 Promoter
R-HSA-76071, RNA Polymerase III Transcription Initiation From Type 3 Promoter
R-HSA-77075, RNA Pol II CTD phosphorylation and interaction with CE
R-HSA-8851708, Signaling by FGFR2 IIIa TM
R-HSA-9018519, Estrogen-dependent gene expression
R-HSA-9670095, Inhibition of DNA recombination at telomere
SIGNORiP19388

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		5434, 799 hits in 994 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		POLR2E, human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		POLR2E

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		5434
PharosiP19388, Tbio

Protein Ontology

More...PROi		PR:P19388
RNActiP19388, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000099817, Expressed in heart left ventricle and 252 other tissues
ExpressionAtlasiP19388, baseline and differential
GenevisibleiP19388, HS

Family and domain databases

Gene3Di3.40.1340.10, 1 hit
3.90.940.20, 1 hit
HAMAPiMF_00025, RNApol_Rpo5_RPB5, 1 hit
InterProiView protein in InterPro
IPR014381, DNA_RNA_pol_RPB5_euk/virus
IPR005571, RNA_pol_Rpb5_N
IPR036710, RNA_pol_Rpb5_N_sf
IPR000783, RNA_pol_subH/Rpb5_C
IPR020608, RNA_pol_subH/Rpb5_CS
IPR039531, Rpb5-like
IPR035913, RPB5-like_sf
IPR020609, RpoH/RPB5
PANTHERiPTHR10535, PTHR10535, 1 hit
PfamiView protein in Pfam
PF01191, RNA_pol_Rpb5_C, 1 hit
PF03871, RNA_pol_Rpb5_N, 1 hit
PIRSFiPIRSF000747, RPB5, 1 hit
SUPFAMiSSF53036, SSF53036, 1 hit
SSF55287, SSF55287, 1 hit
PROSITEiView protein in PROSITE
PS01110, RNA_POL_H_23KD, 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 nameiRPAB1_HUMAN
<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: P19388
Secondary accession number(s): B2R6L4
, D6W5Y1, O43380, Q6PIH5, Q9BT06
<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: November 1, 1990
Last sequence update: October 17, 2006
Last modified: September 29, 2021
This is version 217 of the entry and version 4 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 programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
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