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Protein

DNA-directed RNA polymerase II subunit RPB1

Gene

POLR2A

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. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. 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. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing. Regulation of gene expression levels depends on the balance between methylation and acetylation levels of tha CTD-lysines (By similarity). Initiation or early elongation steps of transcription of growth-factors-induced immediate early genes are regulated by the acetylation status of the CTD (PubMed:24207025). Methylation and dimethylation have a repressive effect on target genes expression (By similarity).By similarity4 Publications
(Microbial infection) Acts as an RNA-dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, acting both as a replicate and transcriptase for the viral RNA circular genome.1 Publication

Miscellaneous

The binding of ribonucleoside triphosphate to the RNA polymerase II transcribing complex probably involves a two-step mechanism. The initial binding seems to occur at the entry (E) site and involves a magnesium ion temporarily coordinated by three conserved aspartate residues of the two largest RNA Pol II subunits. The ribonucleoside triphosphate is transferred by a rotation to the nucleotide addition (A) site for pairing with the template DNA. The catalytic A site involves three conserved aspartate residues of the RNA Pol II largest subunit which permanently coordinate a second magnesium ion.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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 bindingi71Zinc 1By similarity1
Metal bindingi74Zinc 1By similarity1
Metal bindingi81Zinc 1By similarity1
Metal bindingi84Zinc 1By similarity1
Metal bindingi111Zinc 2By similarity1
Metal bindingi114Zinc 2By similarity1
Metal bindingi154Zinc 2By similarity1
Metal bindingi184Zinc 2By similarity1
Metal bindingi495Magnesium 1; catalyticBy similarity1
Metal bindingi495Magnesium 2; shared with RPB2By similarity1
Metal bindingi497Magnesium 1; catalyticBy similarity1
Metal bindingi497Magnesium 2; shared with RPB2By similarity1
Metal bindingi499Magnesium 1; catalyticBy similarity1

<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: ProtInc
  • DNA-directed 5'-3' RNA polymerase activity Source: ProtInc
  • metal ion binding Source: UniProtKB-KW
  • promoter-specific chromatin binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • RNA-directed 5'-3' RNA polymerase activity Source: UniProtKB-KW
  • ubiquitin protein ligase binding Source: BHF-UCL

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

Molecular functionDNA-binding, Nucleotidyltransferase, RNA-directed RNA polymerase, Transferase
Biological processTranscription
LigandMagnesium, Metal-binding, Zinc

Enzyme and pathway databases

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-203927 MicroRNA (miRNA) biogenesis
R-HSA-452723 Transcriptional regulation of pluripotent stem cells
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-73776 RNA Polymerase II Promoter Escape
R-HSA-73779 RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
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-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

SIGNOR Signaling Network Open Resource

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SIGNORi
P24928

<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 RPB1 (EC:2.7.7.6)
Short name:
RNA polymerase II subunit B1
Alternative name(s):
DNA-directed RNA polymerase II subunit A
DNA-directed RNA polymerase III largest subunit
RNA-directed RNA polymerase II subunit RPB1 (EC:2.7.7.48)
<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:POLR2A
Synonyms:POLR2
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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 17

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000181222.14

Human Gene Nomenclature Database

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HGNCi
HGNC:9187 POLR2A

Online Mendelian Inheritance in Man (OMIM)

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MIMi
180660 gene+phenotype

neXtProt; the human protein knowledge platform

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neXtProti
NX_P24928

<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 Cytoskeleton Lysosome 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 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>Mutagenesisi1810R → A: Misexpression of a variety of small nuclear RNAs and small nucleolar RNAs. Loss of interaction with TDRD3 and SMN1/SMN2. 2 Publications1
Mutagenesisi1838K → R: Loss of acetylation and loss of regulation of growth-factor-induced gene expression; when associated with R-1859; R-1866; R-1873; R-1887; R-1908; R-1922 and R-1936. 1 Publication1
Mutagenesisi1859K → R: Loss of acetylation and loss of regulation of growth-factor-induced gene expression; when associated with R-1838; R-1866; R-1873; R-1887; R-1908; R-1922 and R-1936. 1 Publication1
Mutagenesisi1866K → R: Loss of acetylation and loss of regulation of growth-factor-induced gene expression; when associated with R-1859; R-1859; R-1873; R-1887; R-1908; R-1922 and R-1936. 1 Publication1
Mutagenesisi1873K → R: Loss of acetylation and loss of regulation of growth-factor-induced gene expression; when associated with R-1838; R-1859; R-1866; R-1887; R-1908; R-1922 and R-1936. 1 Publication1
Mutagenesisi1887K → R: Loss of acetylation and loss of regulation of growth-factor-induced gene expression; when associated with R-1838; R-1859; R-1866; R-1873; R-1908; R-1922 and R-1936. 1 Publication1
Mutagenesisi1908K → R: Loss of acetylation and loss of regulation of growth-factor-induced gene expression; when associated with R.1838; R-1859; R-1866; R-1873; R-1887; R-1922 and R-1936. 1 Publication1
Mutagenesisi1922K → R: Loss of acetylation and loss of regulation of growth-factor-induced gene expression; when associated with R-1838; R-1859; R-1866; R-1873; R-1887; R-1908 and R-1936. 1 Publication1
Mutagenesisi1936K → R: Loss of acetylation and loss of regulation of growth-factor-induced gene expression; when associated with R-1838; R-1859; R-1866; R-1873; R-1887; R-1908 and R-1922. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
5430
MIMi180660 gene+phenotype

Open Targets

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OpenTargetsi
ENSG00000181222

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA33507

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1641353

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
POLR2A

Domain mapping of disease mutations (DMDM)

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DMDMi
281185484

<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_00000739401 – 1970DNA-directed RNA polymerase II subunit RPB1Add BLAST1970

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 residuei27PhosphoserineCombined sources1
Modified residuei217PhosphoserineCombined sources1
Modified residuei1603Omega-N-methylated arginine; by CARM1; in vitro1 Publication1
Modified residuei1810Asymmetric dimethylarginine; alternate; by CARM12 Publications1
Modified residuei1810Symmetric dimethylarginine; alternate; by PRMT51 Publication1
Modified residuei1838N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei1838N6-methyllysine; alternateBy similarity1
Modified residuei1840Phosphothreonine1 Publication1
Modified residuei1843PhosphoserineCombined sources1 Publication1
Modified residuei1845Phosphoserine1 Publication1
Modified residuei1847PhosphoserineBy similarity1
Modified residuei1849PhosphoserineCombined sources1 Publication1
Modified residuei1850PhosphoserineCombined sources1 Publication1
Modified residuei1854PhosphothreonineCombined sources1
Modified residuei1857Phosphoserine1 Publication1
Modified residuei1859N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei1859N6-methyllysine; alternate1 Publication1
Modified residuei1860Phosphotyrosine1 Publication1
Modified residuei1861Phosphoserine1 Publication1
Modified residuei1863Phosphothreonine1 Publication1
Modified residuei1864PhosphoserineCombined sources1 Publication1
Modified residuei1866N6,N6,N6-trimethyllysine; alternate1 Publication1
Modified residuei1866N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei1866N6-acetyllysine; alternate1 Publication1
Modified residuei1866N6-methyllysine; alternate1 Publication1
Modified residuei1867Phosphotyrosine1 Publication1
Modified residuei1868PhosphoserineCombined sources1
Modified residuei1870Phosphothreonine1 Publication1
Modified residuei1873N6,N6,N6-trimethyllysine; alternate1 Publication1
Modified residuei1873N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei1873N6-methyllysine; alternate1 Publication1
Modified residuei1874PhosphotyrosineCombined sources1 Publication1
Modified residuei1875Phosphoserine1 Publication1
Modified residuei1877Phosphothreonine1 Publication1
Modified residuei1878PhosphoserineCombined sources1 Publication1
Modified residuei1881Phosphotyrosine1 Publication1
Modified residuei1882PhosphoserineCombined sources1 Publication1
Modified residuei1885PhosphothreonineCombined sources1
Modified residuei1887N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei1887N6-acetyllysine; alternate1 Publication1
Modified residuei1887N6-methyllysine; alternate1 Publication1
Modified residuei1894PhosphothreonineBy similarity1
Modified residuei1896PhosphoserineCombined sources1
Modified residuei1899PhosphoserineCombined sources1
Modified residuei1906PhosphoserineCombined sources1
Modified residuei1908N6,N6-dimethyllysineBy similarity1
Modified residuei1909PhosphotyrosineCombined sources1 Publication1
Modified residuei1912Phosphothreonine1 Publication1
Modified residuei1913PhosphoserineCombined sources1 Publication1
Modified residuei1915Phosphothreonine1 Publication1
Modified residuei1916Phosphotyrosine1 Publication1
Modified residuei1917PhosphoserineCombined sources1 Publication1
Modified residuei1919Phosphothreonine1 Publication1
Modified residuei1920PhosphoserineCombined sources1 Publication1
Modified residuei1922N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei1922N6-acetyllysine; alternate1 Publication1
Modified residuei1922N6-methyllysine; alternate1 Publication1
Modified residuei1923PhosphotyrosineCombined sources1 Publication1
Modified residuei1926Phosphothreonine1 Publication1
Modified residuei1927PhosphoserineCombined sources1 Publication1
Modified residuei1929Phosphothreonine1 Publication1
Modified residuei1930Phosphotyrosine1 Publication1
Modified residuei1931PhosphoserineCombined sources1 Publication1
Modified residuei1933Phosphothreonine1 Publication1
Modified residuei1934PhosphoserineCombined sources1
Modified residuei1936N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei1936N6-acetyllysine; alternate1 Publication1
Modified residuei1936N6-methyllysine; alternate1 Publication1

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

The tandem heptapeptide repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat and is mediated, at least, by CDK7 and CDK9. CDK7 phosphorylation of POLR2A associated with DNA promotes transcription initiation by triggering dissociation from DNA. Phosphorylation also takes place at 'Ser-7' of the heptapeptide repeat, which is required for efficient transcription of snRNA genes and processing of the transcripts. The phosphorylation state is believed to result from the balanced action of site-specific CTD kinases and phosphatases, and a 'CTD code' that specifies the position of Pol II within the transcription cycle has been proposed. Dephosphorylated by the protein phosphatase CTDSP1.8 Publications
Among tandem heptapeptide repeats of the C-terminal domain (CTD) some do not match the Y-S-P-T-S-P-S consensus, the seventh serine residue 'Ser-7' being replaced by a lysine. 'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated and dimethylated. EP300 is one of the enzyme able to acetylate 'Lys-7'. Acetylation at 'Lys-7' of non-consensus heptapeptide repeats is associated with 'Ser-2' phosphorylation and active transcription. Regulates initiation or early elongation steps of transcription specially for inducible genes.3 Publications
Methylated at Arg-1810 prior to transcription initiation when the CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808 preventing this methylation. Symmetrically or asymmetrically dimethylated at Arg-1810 by PRMT5 and CARM1 respectively. Symmetric or asymmetric dimethylation modulates interactions with CTD-binding proteins like SMN1/SMN2 and TDRD3. SMN1/SMN2 interacts preferentially with the symmetrically dimethylated form while TDRD3 interacts with the asymmetric form. Through the recruitment of SMN1/SMN2, symmetric dimethylation is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. CTD dimethylation may also facilitate the expression of select RNAs. Among tandem heptapeptide repeats of the C-terminal domain (CTD) some do not match the Y-S-P-T-S-P-S consensus, the seventh serine residue 'Ser-7' being replaced by a lysine. 'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated, dimethylated and trimethylated. Methylation occurs in the earliest transcription stages and precedes or is concomitant to 'Ser-5' and 'Ser-7' phosphorylation. Dimethylation and trimehtylation at 'Lys-7' of non-consensus heptapeptide repeats are exclusively associated with phosphorylated CTD.By similarity3 Publications
Ubiquitinated by WWP2 leading to proteasomal degradation (By similarity). Following UV treatment, the elongating form of RNA polymerase II (RNA pol IIo) is ubiquitinated on UV damage sites without leading to degradation: ubiquitination is facilitated by KIAA1530/UVSSA and promotes RNA pol IIo backtracking to allow access to the nucleotide excision repair machinery.By similarity1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P24928

MaxQB - The MaxQuant DataBase

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MaxQBi
P24928

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

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PaxDbi
P24928

PeptideAtlas

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PeptideAtlasi
P24928

PRoteomics IDEntifications database

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PRIDEi
P24928

ProteomicsDB human proteome resource

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ProteomicsDBi
54240

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P24928

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

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PhosphoSitePlusi
P24928

<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

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Bgeei
ENSG00000181222 Expressed in 222 organ(s), highest expression level in testis

CleanEx database of gene expression profiles

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CleanExi
HS_POLR2A

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P24928 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB012226
CAB016388
CAB022311
HPA021563
HPA053012

<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. Component of a complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active). Interacts (via the C-terminal domain (CTD)) with U2AF2; recruits PRPF19 and the Prp19 complex to the pre-mRNA and may couple transcription to pre-mRNA splicing. Interacts (via the C-terminal domain (CTD)) with SMN1/SMN2; recruits SMN1/SMN2 to RNA Pol II elongation complexes. Interacts via the phosphorylated C-terminal domain with WDR82 and with SETD1A and SETD1B only in the presence of WDR82. When phosphorylated at 'Ser-5', interacts with MEN1; the unphosphorylated form, or phosphorylated at 'Ser-2' does not interact. When phosphorylated at 'Ser-2', interacts with SUPT6H (via SH2 domain). Interacts with RECQL5 and TCEA1; binding of RECQL5 prevents TCEA1 binding. The phosphorylated C-terminal domain interacts with FNBP3 and SYNCRIP. Interacts with ATF7IP. Interacts with DDX5. Interacts with WWP2. Interacts with SETX. Interacts (phosphorylated) with PIH1D1. Interacts (via the C-terminal domain (CTD)) with TDRD3. Interacts with PRMT5. Interacts with XRN2. Interacts with SAFB/SAFB1. Interacts with CCNL1. Interacts with CCNL2, MYO1C, PAF1 and SFRS19. Interacts (via C-terminus) with CMTR1, CTDSP1 and SCAF8. Interacts (via the C-terminal domain (CTD)) with CCNT2 (PubMed:15563843).By similarity26 Publications
(Microbial infection) Interacts with herpes simplex virus 1 protein ICP22; this interaction causes loss of CTD 'Ser-2' phosphorylation from pol II engaged in transcription (PubMed:23029222).1 Publication

<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)

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BioGridi
111426, 299 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P24928

Database of interacting proteins

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DIPi
DIP-29011N

Protein interaction database and analysis system

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IntActi
P24928, 86 interactors

Molecular INTeraction database

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MINTi
P24928

STRING: functional protein association networks

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STRINGi
9606.ENSP00000314949

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P24928

<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

11970
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
P24928

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

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SMRi
P24928

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

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EvolutionaryTracei
P24928

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati1593 – 159917
Repeati1600 – 16062; approximate7
Repeati1608 – 161437
Repeati1615 – 162147
Repeati1622 – 162857
Repeati1629 – 163567
Repeati1636 – 164277
Repeati1643 – 164987
Repeati1650 – 165697
Repeati1657 – 1663107
Repeati1664 – 1670117
Repeati1671 – 1677127
Repeati1678 – 1684137
Repeati1685 – 1691147
Repeati1692 – 1698157
Repeati1699 – 1705167
Repeati1706 – 1712177
Repeati1713 – 1719187
Repeati1720 – 1726197
Repeati1727 – 1733207
Repeati1734 – 1740217
Repeati1741 – 1747227
Repeati1748 – 1754237
Repeati1755 – 1761247
Repeati1762 – 1768257
Repeati1769 – 1775267
Repeati1776 – 1782277
Repeati1783 – 1789287
Repeati1790 – 1796297
Repeati1797 – 1803307
Repeati1804 – 1810317
Repeati1811 – 1817327
Repeati1818 – 1824337
Repeati1825 – 1831347
Repeati1832 – 1838357
Repeati1839 – 1845367
Repeati1846 – 1852377
Repeati1853 – 1859387
Repeati1860 – 1866397
Repeati1867 – 1873407
Repeati1874 – 1880417
Repeati1881 – 1887427
Repeati1888 – 1894437
Repeati1895 – 1901447
Repeati1902 – 1908457
Repeati1909 – 1915467
Repeati1916 – 1922477
Repeati1923 – 1929487
Repeati1930 – 1936497
Repeati1940 – 1946507
Repeati1947 – 195351; approximate7
Repeati1954 – 196052; approximate7

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni833 – 845Bridging helixAdd BLAST13
Regioni1593 – 1960C-terminal domain (CTD); 52 X 7 AA approximate tandem repeats of Y-[ST]-P-[STQ]-[ST]-P-[SRTEVKGN]Add BLAST368

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C-terminal domain (CTD) serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing.1 Publication

<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 RNA polymerase beta' chain family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0260 Eukaryota
COG0086 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00930000151033

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000222975

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG097653

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P24928

KEGG Orthology (KO)

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KOi
K03006

Database for complete collections of gene phylogenies

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PhylomeDBi
P24928

TreeFam database of animal gene trees

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TreeFami
TF103036

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.132.30, 1 hit
3.30.1360.140, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000722 RNA_pol_asu
IPR000684 RNA_pol_II_repeat_euk
IPR006592 RNA_pol_N
IPR007080 RNA_pol_Rpb1_1
IPR007066 RNA_pol_Rpb1_3
IPR007083 RNA_pol_Rpb1_4
IPR007081 RNA_pol_Rpb1_5
IPR007075 RNA_pol_Rpb1_6
IPR007073 RNA_pol_Rpb1_7
IPR038593 RNA_pol_Rpb1_7_sf
IPR038120 Rpb1_funnel_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04997 RNA_pol_Rpb1_1, 1 hit
PF00623 RNA_pol_Rpb1_2, 1 hit
PF04983 RNA_pol_Rpb1_3, 1 hit
PF05000 RNA_pol_Rpb1_4, 1 hit
PF04998 RNA_pol_Rpb1_5, 1 hit
PF04992 RNA_pol_Rpb1_6, 1 hit
PF04990 RNA_pol_Rpb1_7, 1 hit
PF05001 RNA_pol_Rpb1_R, 41 hits

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00663 RPOLA_N, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00115 RNA_POL_II_REPEAT, 42 hits

<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>Sequences (2)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 describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: P24928-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MHGGGPPSGD SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG
60 70 80 90 100
RPKLGGLMDP RQGVIERTGR CQTCAGNMTE CPGHFGHIEL AKPVFHVGFL
110 120 130 140 150
VKTMKVLRCV CFFCSKLLVD SNNPKIKDIL AKSKGQPKKR LTHVYDLCKG
160 170 180 190 200
KNICEGGEEM DNKFGVEQPE GDEDLTKEKG HGGCGRYQPR IRRSGLELYA
210 220 230 240 250
EWKHVNEDSQ EKKILLSPER VHEIFKRISD EECFVLGMEP RYARPEWMIV
260 270 280 290 300
TVLPVPPLSV RPAVVMQGSA RNQDDLTHKL ADIVKINNQL RRNEQNGAAA
310 320 330 340 350
HVIAEDVKLL QFHVATMVDN ELPGLPRAMQ KSGRPLKSLK QRLKGKEGRV
360 370 380 390 400
RGNLMGKRVD FSARTVITPD PNLSIDQVGV PRSIAANMTF AEIVTPFNID
410 420 430 440 450
RLQELVRRGN SQYPGAKYII RDNGDRIDLR FHPKPSDLHL QTGYKVERHM
460 470 480 490 500
CDGDIVIFNR QPTLHKMSMM GHRVRILPWS TFRLNLSVTT PYNADFDGDE
510 520 530 540 550
MNLHLPQSLE TRAEIQELAM VPRMIVTPQS NRPVMGIVQD TLTAVRKFTK
560 570 580 590 600
RDVFLERGEV MNLLMFLSTW DGKVPQPAIL KPRPLWTGKQ IFSLIIPGHI
610 620 630 640 650
NCIRTHSTHP DDEDSGPYKH ISPGDTKVVV ENGELIMGIL CKKSLGTSAG
660 670 680 690 700
SLVHISYLEM GHDITRLFYS NIQTVINNWL LIEGHTIGIG DSIADSKTYQ
710 720 730 740 750
DIQNTIKKAK QDVIEVIEKA HNNELEPTPG NTLRQTFENQ VNRILNDARD
760 770 780 790 800
KTGSSAQKSL SEYNNFKSMV VSGAKGSKIN ISQVIAVVGQ QNVEGKRIPF
810 820 830 840 850
GFKHRTLPHF IKDDYGPESR GFVENSYLAG LTPTEFFFHA MGGREGLIDT
860 870 880 890 900
AVKTAETGYI QRRLIKSMES VMVKYDATVR NSINQVVQLR YGEDGLAGES
910 920 930 940 950
VEFQNLATLK PSNKAFEKKF RFDYTNERAL RRTLQEDLVK DVLSNAHIQN
960 970 980 990 1000
ELEREFERMR EDREVLRVIF PTGDSKVVLP CNLLRMIWNA QKIFHINPRL
1010 1020 1030 1040 1050
PSDLHPIKVV EGVKELSKKL VIVNGDDPLS RQAQENATLL FNIHLRSTLC
1060 1070 1080 1090 1100
SRRMAEEFRL SGEAFDWLLG EIESKFNQAI AHPGEMVGAL AAQSLGEPAT
1110 1120 1130 1140 1150
QMTLNTFHYA GVSAKNVTLG VPRLKELINI SKKPKTPSLT VFLLGQSARD
1160 1170 1180 1190 1200
AERAKDILCR LEHTTLRKVT ANTAIYYDPN PQSTVVAEDQ EWVNVYYEMP
1210 1220 1230 1240 1250
DFDVARISPW LLRVELDRKH MTDRKLTMEQ IAEKINAGFG DDLNCIFNDD
1260 1270 1280 1290 1300
NAEKLVLRIR IMNSDENKMQ EEEEVVDKMD DDVFLRCIES NMLTDMTLQG
1310 1320 1330 1340 1350
IEQISKVYMH LPQTDNKKKI IITEDGEFKA LQEWILETDG VSLMRVLSEK
1360 1370 1380 1390 1400
DVDPVRTTSN DIVEIFTVLG IEAVRKALER ELYHVISFDG SYVNYRHLAL
1410 1420 1430 1440 1450
LCDTMTCRGH LMAITRHGVN RQDTGPLMKC SFEETVDVLM EAAAHGESDP
1460 1470 1480 1490 1500
MKGVSENIML GQLAPAGTGC FDLLLDAEKC KYGMEIPTNI PGLGAAGPTG
1510 1520 1530 1540 1550
MFFGSAPSPM GGISPAMTPW NQGATPAYGA WSPSVGSGMT PGAAGFSPSA
1560 1570 1580 1590 1600
ASDASGFSPG YSPAWSPTPG SPGSPGPSSP YIPSPGGAMS PSYSPTSPAY
1610 1620 1630 1640 1650
EPRSPGGYTP QSPSYSPTSP SYSPTSPSYS PTSPNYSPTS PSYSPTSPSY
1660 1670 1680 1690 1700
SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS
1710 1720 1730 1740 1750
PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPNYSP
1760 1770 1780 1790 1800
TSPNYTPTSP SYSPTSPSYS PTSPNYTPTS PNYSPTSPSY SPTSPSYSPT
1810 1820 1830 1840 1850
SPSYSPSSPR YTPQSPTYTP SSPSYSPSSP SYSPASPKYT PTSPSYSPSS
1860 1870 1880 1890 1900
PEYTPTSPKY SPTSPKYSPT SPKYSPTSPT YSPTTPKYSP TSPTYSPTSP
1910 1920 1930 1940 1950
VYTPTSPKYS PTSPTYSPTS PKYSPTSPTY SPTSPKGSTY SPTSPGYSPT
1960 1970
SPTYSLTSPA ISPDDSDEEN
Length:1,970
Mass (Da):217,176
Last modified:December 15, 2009 - 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:i28D6FD25693A6472
GO
Isoform 2 (identifier: P24928-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     558-566: GEVMNLLMF → VCGPNGNLA
     567-1970: Missing.

Note: No experimental confirmation available.
Show »
Length:566
Mass (Da):63,641
Checksum:i0F3049DAF63F3B20
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 conflicti1067W → L in CAA52862 (PubMed:7622068).Curated1
Sequence conflicti1449D → Y in CAA52862 (PubMed:7622068).Curated1
Sequence conflicti1835A → T in CAA45125 (PubMed:1542581).Curated1
Sequence conflicti1835A → T in CAA52862 (PubMed:7622068).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_051872292R → C. Corresponds to variant dbSNP:rs2229198Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_056184558 – 566GEVMNLLMF → VCGPNGNLA in isoform 2. 1 Publication9
Alternative sequenceiVSP_056185567 – 1970Missing in isoform 2. 1 PublicationAdd BLAST1404

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X63564 mRNA Translation: CAA45125.1
X74874
, X74873, X74872, X74871, X74870 Genomic DNA Translation: CAA52862.1
AC113189 Genomic DNA No translation available.
CH471108 Genomic DNA Translation: EAW90181.1
BC067295 mRNA Translation: AAH67295.1
BC137231 mRNA Translation: AAI37232.1

Protein sequence database of the Protein Information Resource

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PIRi
I38186
S21054

NCBI Reference Sequences

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RefSeqi
NP_000928.1, NM_000937.4

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.270017

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000572844; ENSP00000461879; ENSG00000181222 [P24928-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
5430

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:5430

UCSC genome browser

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UCSCi
uc002ghe.4 human [P24928-1]

Keywords - Coding sequence diversityi

Alternative splicing, 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
X63564 mRNA Translation: CAA45125.1
X74874
, X74873, X74872, X74871, X74870 Genomic DNA Translation: CAA52862.1
AC113189 Genomic DNA No translation available.
CH471108 Genomic DNA Translation: EAW90181.1
BC067295 mRNA Translation: AAH67295.1
BC137231 mRNA Translation: AAI37232.1
PIRiI38186
S21054
RefSeqiNP_000928.1, NM_000937.4
UniGeneiHs.270017

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
2GHQX-ray2.05C/D1795-1803[»]
2GHTX-ray1.80C/D1796-1803[»]
2LTONMR-B1804-1816[»]
3D9KX-ray2.20Y/Z1790-1803[»]
3D9LX-ray2.20Y/Z1790-1803[»]
3D9MX-ray1.75Y/Z1790-1803[»]
3D9NX-ray1.60Y/Z1790-1803[»]
3D9OX-ray2.00Z1790-1803[»]
3D9PX-ray2.10Y/Z1790-1803[»]
4JXTX-ray1.90B1787-1805[»]
5IY6electron microscopy7.20A1-1970[»]
5IY7electron microscopy8.60A1-1970[»]
5IY8electron microscopy7.90A1-1970[»]
5IY9electron microscopy6.30A1-1970[»]
5IYAelectron microscopy5.40A1-1970[»]
5IYBelectron microscopy3.90A1-1970[»]
5IYCelectron microscopy3.90A1-1970[»]
5IYDelectron microscopy3.90A1-1970[»]
5M3HX-ray2.50X/Y1713-1740[»]
5M3JX-ray3.50X1713-1740[»]
ProteinModelPortaliP24928
SMRiP24928
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111426, 299 interactors
CORUMiP24928
DIPiDIP-29011N
IntActiP24928, 86 interactors
MINTiP24928
STRINGi9606.ENSP00000314949

Chemistry databases

BindingDBiP24928
ChEMBLiCHEMBL1641353

PTM databases

iPTMnetiP24928
PhosphoSitePlusiP24928

Polymorphism and mutation databases

BioMutaiPOLR2A
DMDMi281185484

Proteomic databases

EPDiP24928
MaxQBiP24928
PaxDbiP24928
PeptideAtlasiP24928
PRIDEiP24928
ProteomicsDBi54240

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000572844; ENSP00000461879; ENSG00000181222 [P24928-2]
GeneIDi5430
KEGGihsa:5430
UCSCiuc002ghe.4 human [P24928-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5430
DisGeNETi5430
EuPathDBiHostDB:ENSG00000181222.14

GeneCards: human genes, protein and diseases

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GeneCardsi
POLR2A

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0173727
HGNCiHGNC:9187 POLR2A
HPAiCAB012226
CAB016388
CAB022311
HPA021563
HPA053012
MIMi180660 gene+phenotype
neXtProtiNX_P24928
OpenTargetsiENSG00000181222
PharmGKBiPA33507

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0260 Eukaryota
COG0086 LUCA
GeneTreeiENSGT00930000151033
HOGENOMiHOG000222975
HOVERGENiHBG097653
InParanoidiP24928
KOiK03006
PhylomeDBiP24928
TreeFamiTF103036

Enzyme and pathway databases

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-203927 MicroRNA (miRNA) biogenesis
R-HSA-452723 Transcriptional regulation of pluripotent stem cells
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-73776 RNA Polymerase II Promoter Escape
R-HSA-73779 RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
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-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
SIGNORiP24928

Miscellaneous databases

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

More...
ChiTaRSi
POLR2A human
EvolutionaryTraceiP24928

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
POLR2A

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

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GenomeRNAii
5430

Protein Ontology

More...
PROi
PR:P24928

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000181222 Expressed in 222 organ(s), highest expression level in testis
CleanExiHS_POLR2A
GenevisibleiP24928 HS

Family and domain databases

Gene3Di1.10.132.30, 1 hit
3.30.1360.140, 1 hit
InterProiView protein in InterPro
IPR000722 RNA_pol_asu
IPR000684 RNA_pol_II_repeat_euk
IPR006592 RNA_pol_N
IPR007080 RNA_pol_Rpb1_1
IPR007066 RNA_pol_Rpb1_3
IPR007083 RNA_pol_Rpb1_4
IPR007081 RNA_pol_Rpb1_5
IPR007075 RNA_pol_Rpb1_6
IPR007073 RNA_pol_Rpb1_7
IPR038593 RNA_pol_Rpb1_7_sf
IPR038120 Rpb1_funnel_sf
PfamiView protein in Pfam
PF04997 RNA_pol_Rpb1_1, 1 hit
PF00623 RNA_pol_Rpb1_2, 1 hit
PF04983 RNA_pol_Rpb1_3, 1 hit
PF05000 RNA_pol_Rpb1_4, 1 hit
PF04998 RNA_pol_Rpb1_5, 1 hit
PF04992 RNA_pol_Rpb1_6, 1 hit
PF04990 RNA_pol_Rpb1_7, 1 hit
PF05001 RNA_pol_Rpb1_R, 41 hits
SMARTiView protein in SMART
SM00663 RPOLA_N, 1 hit
PROSITEiView protein in PROSITE
PS00115 RNA_POL_II_REPEAT, 42 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiRPB1_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: P24928
Secondary accession number(s): A6NN93, B9EH88, Q6NX41
<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: March 1, 1992
Last sequence update: December 15, 2009
Last modified: December 5, 2018
This is version 207 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 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, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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