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UniProtKB - P52434 (RPAB3_HUMAN)

Entry version 192 (13 Feb 2019)
Sequence version 4 (23 Jan 2007)
Previous versions | rss
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Protein

DNA-directed RNA polymerases I, II, and III subunit RPABC3

Gene

POLR2H

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.1 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-directed 5'-3' RNA polymerase activity Source: UniProtKB-KW
  • single-stranded DNA binding Source: CAFA
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the 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

Molecular functionDNA-binding
Biological processTranscription

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-1834949 Cytosolic sensors of pathogen-associated DNA
R-HSA-203927 MicroRNA (miRNA) biogenesis
R-HSA-427413 NoRC negatively regulates rRNA expression
R-HSA-452723 Transcriptional regulation of pluripotent stem cells
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-73777 RNA Polymerase I Chain Elongation
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

<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 RPABC3
Short name:
RNA polymerases I, II, and III subunit ABC3
Alternative name(s):
DNA-directed RNA polymerase II subunit H
DNA-directed RNA polymerases I, II, and III 17.1 kDa polypeptide
RPB17
RPB8 homolog
Short name:
hRPB8
<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:POLR2H
<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 3

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000163882.9

Human Gene Nomenclature Database

More...HGNCi		HGNC:9195 POLR2H

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		606023 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P52434

<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

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		5437

Open Targets

More...OpenTargetsi		ENSG00000163882

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33515

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		POLR2H

Domain mapping of disease mutations (DMDM)

More...DMDMi		20178325

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<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_00000739972 – 150DNA-directed RNA polymerases I, II, and III subunit RPABC3Add BLAST149

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P52434

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P52434

MaxQB - The MaxQuant DataBase

More...MaxQBi		P52434

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

More...PaxDbi		P52434

PeptideAtlas

More...PeptideAtlasi		P52434

PRoteomics IDEntifications database

More...PRIDEi		P52434

ProteomicsDB human proteome resource

More...ProteomicsDBi		56485

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P52434-1 [P52434-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P52434

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

More...PhosphoSitePlusi		P52434

<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		ENSG00000163882 Expressed in 228 organ(s), highest expression level in mucosa of transverse colon

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P52434 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P52434 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA037745
HPA055813

<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. Directly interacts with POLR2A.3 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		111433, 78 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P52434

Database of interacting proteins

More...DIPi		DIP-27556N

Protein interaction database and analysis system

More...IntActi		P52434, 21 interactors

Molecular INTeraction database

More...MINTi		P52434

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000296223

<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

1150
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F3INMR-A1-150[»]
5IY6electron microscopy7.20H1-150[»]
5IY7electron microscopy8.60H1-150[»]
5IY8electron microscopy7.90H1-150[»]
5IY9electron microscopy6.30H1-150[»]
5IYAelectron microscopy5.40H1-150[»]
5IYBelectron microscopy3.90H1-150[»]
5IYCelectron microscopy3.90H1-150[»]
5IYDelectron microscopy3.90H1-150[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P52434

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

More...SMRi		P52434

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P52434

<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

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>Regioni16 – 40Non-specific ssDNA bindingAdd BLAST25

<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 eukaryotic RPB8 RNA polymerase subunit family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3400 Eukaryota
ENOG4111FT0 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00390000018195

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000175572

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG036116

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P52434

KEGG Orthology (KO)

More...KOi		K03016

Identification of Orthologs from Complete Genome Data

More...OMAi		RVQATSH

Database of Orthologous Groups

More...OrthoDBi		1504067at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P52434

TreeFam database of animal gene trees

More...TreeFami		TF103043

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR012340 NA-bd_OB-fold
IPR005570 RNA_pol_Rpb8

The PANTHER Classification System

More...PANTHERi		PTHR10917 PTHR10917, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF03870 RNA_pol_Rpb8, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000779 RNA_pol_Rpb8, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00658 RPOL8c, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50249 SSF50249, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (5+)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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 <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

This entry has 5 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P52434-1) [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
MAGILFEDIF DVKDIDPEGK KFDRVSRLHC ESESFKMDLI LDVNIQIYPV 
        60         70         80         90        100
DLGDKFRLVI ASTLYEDGTL DDGEYNPTDD RPSRADQFEY VMYGKVYRIE 
       110        120        130        140        150
GDETSTEAAT RLSAYVSYGG LLMRLQGDAN NLHGFEVDSR VYLLMKKLAF
Length:150
Mass (Da):17,143
Last modified:January 23, 2007 - 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:i944D0860809F1425
GO
Isoform 2 (identifier: P52434-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     84-112: RADQFEYVMYGKVYRIEGDETSTEAATRL → S

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:122
Mass (Da):13,849
Checksum:i67D60212F40AC1DC
GO
Isoform 3 (identifier: P52434-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:114
Mass (Da):12,959
Checksum:i6ED22DDC8CC5EB96
GO
Isoform 4 (identifier: P52434-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     113-150: SAYVSYGGLL...VYLLMKKLAF → LRLRAAEWQC...DEEASLLNLA

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:175
Mass (Da):19,767
Checksum:i2544A688EC043228
GO
Isoform 5 (identifier: P52434-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: Missing.
     84-112: RADQFEYVMYGKVYRIEGDETSTEAATRL → S

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:86
Mass (Da):9,664
Checksum:iB038E50425F19FCF
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9JLU1C9JLU1_HUMAN
DNA-directed RNA polymerases I, II,...
POLR2H
148Annotation 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>
C9JJJ9C9JJJ9_HUMAN
DNA-directed RNA polymerases I, II,...
POLR2H
11Annotation 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 conflicti19G → A in AAA91458 (PubMed:8524256).Curated1

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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0550171 – 36Missing in isoform 3 and isoform 5. CuratedAdd BLAST36
Alternative sequenceiVSP_05501884 – 112RADQF…AATRL → S in isoform 2 and isoform 5. CuratedAdd BLAST29
Alternative sequenceiVSP_055019113 – 150SAYVS…KKLAF → LRLRAAEWQCSRITGWGLLF QLCVRVLWGPAHEAAGGCQQ PAWIRGGLQSLSPDEEASLL NLA in isoform 4. CuratedAdd BLAST38

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
U37689 mRNA Translation: AAA91458.1
Z49199 mRNA Translation: CAA89060.1
AJ252079, AJ252080 Genomic DNA Translation: CAB92189.1
AC078797 Genomic DNA No translation available.
BC000739 mRNA Translation: AAH00739.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS3264.1 [P52434-1]
CCDS63859.1 [P52434-4]
CCDS63860.1 [P52434-2]
CCDS63861.1 [P52434-3]
CCDS63862.1 [P52434-5]

Protein sequence database of the Protein Information Resource

More...PIRi		S55370

NCBI Reference Sequences

More...RefSeqi		NP_001265627.1, NM_001278698.1 [P52434-4]
NP_001265628.1, NM_001278699.2 [P52434-3]
NP_001265629.1, NM_001278700.1 [P52434-3]
NP_001265643.1, NM_001278714.1 [P52434-2]
NP_001265644.1, NM_001278715.1 [P52434-5]
NP_006223.2, NM_006232.4 [P52434-1]
XP_006713729.1, XM_006713666.2 [P52434-4]
XP_006713730.1, XM_006713667.2 [P52434-4]
XP_016862125.1, XM_017006636.1 [P52434-2]
XP_016862126.1, XM_017006637.1 [P52434-5]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.432574

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000429568; ENSP00000415536; ENSG00000163882 [P52434-4]
ENST00000430783; ENSP00000411883; ENSG00000163882 [P52434-2]
ENST00000438240; ENSP00000398622; ENSG00000163882 [P52434-3]
ENST00000443489; ENSP00000393773; ENSG00000163882 [P52434-5]
ENST00000452961; ENSP00000399882; ENSG00000163882 [P52434-3]
ENST00000456318; ENSP00000392913; ENSG00000163882 [P52434-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5437

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5437

UCSC genome browser

More...UCSCi		uc032smc.2 human [P52434-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
U37689 mRNA Translation: AAA91458.1
Z49199 mRNA Translation: CAA89060.1
AJ252079, AJ252080 Genomic DNA Translation: CAB92189.1
AC078797 Genomic DNA No translation available.
BC000739 mRNA Translation: AAH00739.1
CCDSiCCDS3264.1 [P52434-1]
CCDS63859.1 [P52434-4]
CCDS63860.1 [P52434-2]
CCDS63861.1 [P52434-3]
CCDS63862.1 [P52434-5]
PIRiS55370
RefSeqiNP_001265627.1, NM_001278698.1 [P52434-4]
NP_001265628.1, NM_001278699.2 [P52434-3]
NP_001265629.1, NM_001278700.1 [P52434-3]
NP_001265643.1, NM_001278714.1 [P52434-2]
NP_001265644.1, NM_001278715.1 [P52434-5]
NP_006223.2, NM_006232.4 [P52434-1]
XP_006713729.1, XM_006713666.2 [P52434-4]
XP_006713730.1, XM_006713667.2 [P52434-4]
XP_016862125.1, XM_017006636.1 [P52434-2]
XP_016862126.1, XM_017006637.1 [P52434-5]
UniGeneiHs.432574

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F3INMR-A1-150[»]
5IY6electron microscopy7.20H1-150[»]
5IY7electron microscopy8.60H1-150[»]
5IY8electron microscopy7.90H1-150[»]
5IY9electron microscopy6.30H1-150[»]
5IYAelectron microscopy5.40H1-150[»]
5IYBelectron microscopy3.90H1-150[»]
5IYCelectron microscopy3.90H1-150[»]
5IYDelectron microscopy3.90H1-150[»]
ProteinModelPortaliP52434
SMRiP52434
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111433, 78 interactors
CORUMiP52434
DIPiDIP-27556N
IntActiP52434, 21 interactors
MINTiP52434
STRINGi9606.ENSP00000296223

PTM databases

iPTMnetiP52434
PhosphoSitePlusiP52434

Polymorphism and mutation databases

BioMutaiPOLR2H
DMDMi20178325

Proteomic databases

EPDiP52434
jPOSTiP52434
MaxQBiP52434
PaxDbiP52434
PeptideAtlasiP52434
PRIDEiP52434
ProteomicsDBi56485
TopDownProteomicsiP52434-1 [P52434-1]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		5437
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000429568; ENSP00000415536; ENSG00000163882 [P52434-4]
ENST00000430783; ENSP00000411883; ENSG00000163882 [P52434-2]
ENST00000438240; ENSP00000398622; ENSG00000163882 [P52434-3]
ENST00000443489; ENSP00000393773; ENSG00000163882 [P52434-5]
ENST00000452961; ENSP00000399882; ENSG00000163882 [P52434-3]
ENST00000456318; ENSP00000392913; ENSG00000163882 [P52434-1]
GeneIDi5437
KEGGihsa:5437
UCSCiuc032smc.2 human [P52434-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5437
DisGeNETi5437
EuPathDBiHostDB:ENSG00000163882.9

GeneCards: human genes, protein and diseases

More...GeneCardsi		POLR2H
HGNCiHGNC:9195 POLR2H
HPAiHPA037745
HPA055813
MIMi606023 gene
neXtProtiNX_P52434
OpenTargetsiENSG00000163882
PharmGKBiPA33515

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3400 Eukaryota
ENOG4111FT0 LUCA
GeneTreeiENSGT00390000018195
HOGENOMiHOG000175572
HOVERGENiHBG036116
InParanoidiP52434
KOiK03016
OMAiRVQATSH
OrthoDBi1504067at2759
PhylomeDBiP52434
TreeFamiTF103043

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-1834949 Cytosolic sensors of pathogen-associated DNA
R-HSA-203927 MicroRNA (miRNA) biogenesis
R-HSA-427413 NoRC negatively regulates rRNA expression
R-HSA-452723 Transcriptional regulation of pluripotent stem cells
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-73777 RNA Polymerase I Chain Elongation
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

Miscellaneous databases

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

More...ChiTaRSi		POLR2H human
EvolutionaryTraceiP52434

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		POLR2H

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

More...GenomeRNAii		5437

Protein Ontology

More...PROi		PR:P52434

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000163882 Expressed in 228 organ(s), highest expression level in mucosa of transverse colon
ExpressionAtlasiP52434 baseline and differential
GenevisibleiP52434 HS

Family and domain databases

InterProiView protein in InterPro
IPR012340 NA-bd_OB-fold
IPR005570 RNA_pol_Rpb8
PANTHERiPTHR10917 PTHR10917, 1 hit
PfamiView protein in Pfam
PF03870 RNA_pol_Rpb8, 1 hit
PIRSFiPIRSF000779 RNA_pol_Rpb8, 1 hit
SMARTiView protein in SMART
SM00658 RPOL8c, 1 hit
SUPFAMiSSF50249 SSF50249, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRPAB3_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: P52434
Secondary accession number(s): C9J413
, C9JBJ6, C9JCU7, C9JUA8, P53802, Q969R0
<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: October 1, 1996
Last sequence update: January 23, 2007
Last modified: February 13, 2019
This is version 192 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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