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UniProtKB - P08518 (RPB2_YEAST)

Entry version 222 (29 Sep 2021)
Sequence version 2 (01 Nov 1997)
Previous versions | rss
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Protein

DNA-directed RNA polymerase II subunit RPB2

Gene

RPB2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest component of RNA polymerases II which synthesizes mRNA precursors and many functional non-coding RNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. During a transcription cycle, Pol II, general transcription factors and the Mediator complex assemble as the preinitiation complex (PIC) at the promoter. 11-15 base pairs of DNA surrounding the transcription start site are melted and the single-stranded DNA template strand of the promoter is positioned deeply within the central active site cleft of Pol II to form the open complex. After synthesis of about 30 bases of RNA, Pol II releases its contacts with the core promoter and the rest of the transcription machinery (promoter clearance) and enters the stage of transcription elongation in which it moves on the template as the transcript elongates. Pol II appears to oscillate between inactive and active conformations at each step of nucleotide addition. Pol II is composed of mobile elements that move relative to each other. The core element with the central large cleft comprises RPB3, RBP10, RPB11, RPB12 and regions of RPB1 and RPB2 forming the active center. The clamp element (portions of RPB1, RPB2 and RPB3) is connected to the core through a set of flexible switches and moves to open and close the cleft. The cleft is surrounded by jaws: an upper jaw formed by portions of RBP1, RPB2 and RPB9, and a lower jaw. The jaws are thought to grab the incoming DNA template. The fork loop 1 (RPB2) interacts with the RNA-DNA hybrid, possibly stabilizing it.

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 coordinated by three conserved aspartate residues of the two largest RNA Pol II subunits.
Present with 18700 molecules/cell in log phase SD medium.1 Publication

<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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi837Magnesium; shared with RPB11
Metal bindingi1163Zinc1
Metal bindingi1166Zinc1
Metal bindingi1182Zinc1
Metal bindingi1185Zinc1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri1163 – 1185C4-typeAdd BLAST23

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

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 functionNucleotidyltransferase, Transferase
Biological processTranscription
LigandMagnesium, Metal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-113418, Formation of the Early Elongation Complex
R-SCE-674695, RNA Polymerase II Pre-transcription Events
R-SCE-6781823, Formation of TC-NER Pre-Incision Complex
R-SCE-6782135, Dual incision in TC-NER
R-SCE-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-SCE-6796648, TP53 Regulates Transcription of DNA Repair Genes
R-SCE-6807505, RNA polymerase II transcribes snRNA genes
R-SCE-72086, mRNA Capping
R-SCE-73776, RNA Polymerase II Promoter Escape
R-SCE-73779, RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
R-SCE-75953, RNA Polymerase II Transcription Initiation
R-SCE-75955, RNA Polymerase II Transcription Elongation
R-SCE-76042, RNA Polymerase II Transcription Initiation And Promoter Clearance
R-SCE-77075, RNA Pol II CTD phosphorylation and interaction with CE
R-SCE-9018519, Estrogen-dependent gene expression

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA-directed RNA polymerase II subunit RPB2 (EC:2.7.7.6)
Short name:
RNA polymerase II subunit 2
Alternative name(s):
B150
DNA-directed RNA polymerase II 140 kDa polypeptide
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RPB2
Synonyms:RPB150, RPO22
Ordered Locus Names:YOR151C
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XV

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000005677, RPB2

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YOR151C

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000480911 – 1224DNA-directed RNA polymerase II subunit RPB2Add BLAST1224

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 residuei919PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P08518

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

More...PaxDbi		P08518

PRoteomics IDEntifications database

More...PRIDEi		P08518

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P08518

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits.

3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		34547, 471 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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

Database of interacting proteins

More...DIPi		DIP-14N

Protein interaction database and analysis system

More...IntActi		P08518, 95 interactors

Molecular INTeraction database

More...MINTi		P08518

STRING: functional protein association networks

More...STRINGi		4932.YOR151C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P08518, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11224
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P08518

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P08518

<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>Regioni467 – 478Fork loop 1Add BLAST12

<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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1163 – 1185C4-typeAdd BLAST23

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0214, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00950000183132

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000524_5_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P08518

Identification of Orthologs from Complete Genome Data

More...OMAi		EIMYNGH

Family and domain databases

Conserved Domains Database

More...CDDi		cd00653, RNA_pol_B_RPB2, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.40.270.10, 1 hit
2.40.50.150, 1 hit
3.90.1110.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR015712, DNA-dir_RNA_pol_su2
IPR007120, DNA-dir_RNAP_su2_dom
IPR037033, DNA-dir_RNAP_su2_hyb_sf
IPR007121, RNA_pol_bsu_CS
IPR007644, RNA_pol_bsu_protrusion
IPR007642, RNA_pol_Rpb2_2
IPR037034, RNA_pol_Rpb2_2_sf
IPR007645, RNA_pol_Rpb2_3
IPR007646, RNA_pol_Rpb2_4
IPR007647, RNA_pol_Rpb2_5
IPR007641, RNA_pol_Rpb2_7
IPR014724, RNA_pol_RPB2_OB-fold

The PANTHER Classification System

More...PANTHERi		PTHR20856, PTHR20856, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF04563, RNA_pol_Rpb2_1, 1 hit
PF04561, RNA_pol_Rpb2_2, 1 hit
PF04565, RNA_pol_Rpb2_3, 1 hit
PF04566, RNA_pol_Rpb2_4, 1 hit
PF04567, RNA_pol_Rpb2_5, 1 hit
PF00562, RNA_pol_Rpb2_6, 1 hit
PF04560, RNA_pol_Rpb2_7, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS01166, RNA_POL_BETA, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P08518-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSDLANSEKY YDEDPYGFED ESAPITAEDS WAVISAFFRE KGLVSQQLDS 
        60         70         80         90        100
FNQFVDYTLQ DIICEDSTLI LEQLAQHTTE SDNISRKYEI SFGKIYVTKP 
       110        120        130        140        150
MVNESDGVTH ALYPQEARLR NLTYSSGLFV DVKKRTYEAI DVPGRELKYE 
       160        170        180        190        200
LIAEESEDDS ESGKVFIGRL PIMLRSKNCY LSEATESDLY KLKECPFDMG 
       210        220        230        240        250
GYFIINGSEK VLIAQERSAG NIVQVFKKAA PSPISHVAEI RSALEKGSRF 
       260        270        280        290        300
ISTLQVKLYG REGSSARTIK ATLPYIKQDI PIVIIFRALG IIPDGEILEH 
       310        320        330        340        350
ICYDVNDWQM LEMLKPCVED GFVIQDRETA LDFIGRRGTA LGIKKEKRIQ 
       360        370        380        390        400
YAKDILQKEF LPHITQLEGF ESRKAFFLGY MINRLLLCAL DRKDQDDRDH 
       410        420        430        440        450
FGKKRLDLAG PLLAQLFKTL FKKLTKDIFR YMQRTVEEAH DFNMKLAINA 
       460        470        480        490        500
KTITSGLKYA LATGNWGEQK KAMSSRAGVS QVLNRYTYSS TLSHLRRTNT 
       510        520        530        540        550
PIGRDGKLAK PRQLHNTHWG LVCPAETPEG QACGLVKNLS LMSCISVGTD 
       560        570        580        590        600
PMPIITFLSE WGMEPLEDYV PHQSPDATRV FVNGVWHGVH RNPARLMETL 
       610        620        630        640        650
RTLRRKGDIN PEVSMIRDIR EKELKIFTDA GRVYRPLFIV EDDESLGHKE 
       660        670        680        690        700
LKVRKGHIAK LMATEYQDIE GGFEDVEEYT WSSLLNEGLV EYIDAEEEES 
       710        720        730        740        750
ILIAMQPEDL EPAEANEEND LDVDPAKRIR VSHHATTFTH CEIHPSMILG 
       760        770        780        790        800
VAASIIPFPD HNQSPRNTYQ SAMGKQAMGV FLTNYNVRMD TMANILYYPQ 
       810        820        830        840        850
KPLGTTRAME YLKFRELPAG QNAIVAIACY SGYNQEDSMI MNQSSIDRGL 
       860        870        880        890        900
FRSLFFRSYM DQEKKYGMSI TETFEKPQRT NTLRMKHGTY DKLDDDGLIA 
       910        920        930        940        950
PGVRVSGEDV IIGKTTPISP DEEELGQRTA YHSKRDASTP LRSTENGIVD 
       960        970        980        990       1000
QVLVTTNQDG LKFVKVRVRT TKIPQIGDKF ASRHGQKGTI GITYRREDMP 
      1010       1020       1030       1040       1050
FTAEGIVPDL IINPHAIPSR MTVAHLIECL LSKVAALSGN EGDASPFTDI 
      1060       1070       1080       1090       1100
TVEGISKLLR EHGYQSRGFE VMYNGHTGKK LMAQIFFGPT YYQRLRHMVD 
      1110       1120       1130       1140       1150
DKIHARARGP MQVLTRQPVE GRSRDGGLRF GEMERDCMIA HGAASFLKER 
      1160       1170       1180       1190       1200
LMEASDAFRV HICGICGLMT VIAKLNHNQF ECKGCDNKID IYQIHIPYAA 
      1210       1220 
KLLFQELMAM NITPRLYTDR SRDF
Length:1,224
Mass (Da):138,751
Last modified:November 1, 1997 - 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:iBABD03212C0A583E
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 conflicti1003 – 1006AEGI → RRRY in AAA68096 (PubMed:3547406).Curated4

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
M15693 Genomic DNA Translation: AAA68096.1
U55020 Genomic DNA Translation: AAC49637.1
Z75059 Genomic DNA Translation: CAA99357.1
AF527884 Genomic DNA Translation: AAP57849.1
BK006948 Genomic DNA Translation: DAA10924.1

Protein sequence database of the Protein Information Resource

More...PIRi		A25884

NCBI Reference Sequences

More...RefSeqi		NP_014794.3, NM_001183570.3

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YOR151C_mRNA; YOR151C; YOR151C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		854322

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YOR151C

<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
M15693 Genomic DNA Translation: AAA68096.1
U55020 Genomic DNA Translation: AAC49637.1
Z75059 Genomic DNA Translation: CAA99357.1
AF527884 Genomic DNA Translation: AAP57849.1
BK006948 Genomic DNA Translation: DAA10924.1
PIRiA25884
RefSeqiNP_014794.3, NM_001183570.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I3QX-ray3.10B1-1224[»]
1I50X-ray2.80B1-1224[»]
1I6HX-ray3.30B1-1224[»]
1K83X-ray2.80B1-1224[»]
1NIKX-ray4.10B1-1224[»]
1NT9X-ray4.20B1-1224[»]
1PQVX-ray3.80B1-1224[»]
1R5UX-ray4.50B1-1224[»]
1R9SX-ray4.25B1-1224[»]
1R9TX-ray3.50B1-1224[»]
1SFOX-ray3.61B1-1224[»]
1TWAX-ray3.20B1-1224[»]
1TWCX-ray3.00B1-1224[»]
1TWFX-ray2.30B1-1224[»]
1TWGX-ray3.30B1-1224[»]
1TWHX-ray3.40B1-1224[»]
1WCMX-ray3.80B1-1224[»]
1Y1VX-ray3.80B1-1224[»]
1Y1WX-ray4.00B1-1224[»]
1Y1YX-ray4.00B1-1224[»]
1Y77X-ray4.50B1-1224[»]
2B63X-ray3.80B1-1224[»]
2B8KX-ray4.15B1-1224[»]
2E2HX-ray3.95B1-1224[»]
2E2IX-ray3.41B1-1224[»]
2E2JX-ray3.50B1-1224[»]
2JA5X-ray3.80B1-1224[»]
2JA6X-ray4.00B1-1224[»]
2JA7X-ray3.80B/N1-1224[»]
2JA8X-ray3.80B1-1224[»]
2NVQX-ray2.90B1-1224[»]
2NVTX-ray3.36B1-1224[»]
2NVXX-ray3.60B1-1224[»]
2NVYX-ray3.40B1-1224[»]
2NVZX-ray4.30B1-1224[»]
2R7ZX-ray3.80B1-1224[»]
2R92X-ray3.80B1-1224[»]
2R93X-ray4.00B1-1224[»]
2VUMX-ray3.40B1-1224[»]
2YU9X-ray3.40B1-1224[»]
3CQZX-ray2.80B1-1223[»]
3FKIX-ray3.88B1-1224[»]
3GTGX-ray3.78B1-1224[»]
3GTJX-ray3.42B1-1224[»]
3GTKX-ray3.80B1-1224[»]
3GTLX-ray3.38B1-1224[»]
3GTMX-ray3.80B1-1224[»]
3GTOX-ray4.00B1-1224[»]
3GTPX-ray3.90B1-1224[»]
3GTQX-ray3.80B1-1224[»]
3H3VX-ray4.00C1-1224[»]
3HOUX-ray3.20B/N1-1224[»]
3HOVX-ray3.50B1-1224[»]
3HOWX-ray3.60B1-1224[»]
3HOXX-ray3.65B1-1224[»]
3HOYX-ray3.40B1-1224[»]
3HOZX-ray3.65B1-1224[»]
3I4MX-ray3.70B1-1224[»]
3I4NX-ray3.90B1-1224[»]
3J0Kelectron microscopy36.00B1-1224[»]
3J1Nelectron microscopy16.00B1-1224[»]
3K1FX-ray4.30B1-1224[»]
3K7AX-ray3.80B1-1224[»]
3M3YX-ray3.18B1-1224[»]
3M4OX-ray3.57B1-1224[»]
3PO2X-ray3.30B1-1224[»]
3PO3X-ray3.30B1-1224[»]
3QT1X-ray4.30B1-1224[»]
3RZDX-ray3.30B1-1224[»]
3RZOX-ray3.00B1-1224[»]
3S14X-ray2.85B1-1224[»]
3S15X-ray3.30B1-1224[»]
3S16X-ray3.24B1-1224[»]
3S17X-ray3.20B1-1224[»]
3S1MX-ray3.13B1-1224[»]
3S1NX-ray3.10B1-1224[»]
3S1QX-ray3.30B1-1224[»]
3S1RX-ray3.20B1-1224[»]
3S2DX-ray3.20B1-1224[»]
3S2HX-ray3.30B1-1224[»]
4A3BX-ray3.50B1-1224[»]
4A3CX-ray3.50B1-1224[»]
4A3DX-ray3.40B1-1224[»]
4A3EX-ray3.40B1-1224[»]
4A3FX-ray3.50B1-1224[»]
4A3GX-ray3.50B1-1224[»]
4A3IX-ray3.80B1-1224[»]
4A3JX-ray3.70B1-1224[»]
4A3KX-ray3.50B1-1224[»]
4A3LX-ray3.50B1-1224[»]
4A3MX-ray3.90B1-1224[»]
4A93X-ray3.40B1-1224[»]
4BBRX-ray3.40B1-1224[»]
4BBSX-ray3.60B1-1224[»]
4BXXX-ray3.28B1-1224[»]
4BXZX-ray4.80B1-1224[»]
4BY1X-ray3.60B1-1224[»]
4BY7X-ray3.15B1-1224[»]
4V1Melectron microscopy6.60B1-1224[»]
4V1Nelectron microscopy7.80B1-1224[»]
4V1Oelectron microscopy9.70B1-1224[»]
4X67X-ray4.10B1-1224[»]
4X6AX-ray3.96B1-1224[»]
4Y52X-ray3.50B1-1224[»]
4Y7NX-ray3.30B1-1224[»]
5C3EX-ray3.70B1-1224[»]
5C44X-ray3.95B1-1224[»]
5C4AX-ray4.20B1-1224[»]
5C4JX-ray4.00B1-1224[»]
5C4XX-ray4.00B1-1224[»]
5FMFelectron microscopy6.00B1-1224[»]
5FYWelectron microscopy4.35B1-1224[»]
5FZ5electron microscopy8.80B1-1224[»]
5IP7X-ray3.52B2-1224[»]
5IP9X-ray3.90B2-1224[»]
5OQJelectron microscopy4.70B1-1224[»]
5OQMelectron microscopy5.80B1-1224[»]
5OT2X-ray3.20B1-1224[»]
5SVAelectron microscopy15.30B1-1224[»]
5U5QX-ray3.80B1-1224[»]
5VVRelectron microscopy5.80B1-1224[»]
5VVSelectron microscopy6.40B1-1224[»]
5W4UX-ray3.60B1-1224[»]
5W51X-ray3.40B1-1224[»]
6BLOX-ray3.40B1-1224[»]
6BLPX-ray3.20B1-1224[»]
6BM2X-ray3.40B1-1224[»]
6BM4X-ray2.95B1-1224[»]
6BQFX-ray3.35B1-1224[»]
6GYKelectron microscopy5.10B1-1224[»]
6GYLelectron microscopy4.80B1-1224[»]
6GYMelectron microscopy6.70B1-1224[»]
6I84electron microscopy4.40B1-1224[»]
6O6Celectron microscopy3.10B1-1224[»]
6UPXX-ray3.40B1-1224[»]
6UPYX-ray3.40B1-1224[»]
6UPZX-ray3.10B1-1224[»]
6UQ0X-ray3.56B1-1224[»]
6UQ1X-ray3.60B1-1224[»]
6UQ2X-ray3.20B1-1224[»]
6UQ3X-ray3.47B1-1224[»]
7KEDX-ray3.60B1-1224[»]
7KEEX-ray3.45B1-1224[»]
7KEFX-ray3.89B1-1224[»]
7O4Ielectron microscopy3.20B1-1224[»]
7O4Jelectron microscopy2.90B1-1224[»]
7O4Kelectron microscopy3.60B1-1224[»]
7O4Lelectron microscopy3.40B1-1224[»]
7O72electron microscopy3.40B1-1224[»]
7O73electron microscopy3.40B1-1224[»]
7O75electron microscopy3.20B1-1224[»]
SMRiP08518
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi34547, 471 interactors
ComplexPortaliCPX-2662, DNA-directed RNA polymerase II complex
DIPiDIP-14N
IntActiP08518, 95 interactors
MINTiP08518
STRINGi4932.YOR151C

PTM databases

iPTMnetiP08518

Proteomic databases

MaxQBiP08518
PaxDbiP08518
PRIDEiP08518

Genome annotation databases

EnsemblFungiiYOR151C_mRNA; YOR151C; YOR151C
GeneIDi854322
KEGGisce:YOR151C

Organism-specific databases

SGDiS000005677, RPB2
VEuPathDBiFungiDB:YOR151C

Phylogenomic databases

eggNOGiKOG0214, Eukaryota
GeneTreeiENSGT00950000183132
HOGENOMiCLU_000524_5_1_1
InParanoidiP08518
OMAiEIMYNGH

Enzyme and pathway databases

ReactomeiR-SCE-113418, Formation of the Early Elongation Complex
R-SCE-674695, RNA Polymerase II Pre-transcription Events
R-SCE-6781823, Formation of TC-NER Pre-Incision Complex
R-SCE-6782135, Dual incision in TC-NER
R-SCE-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-SCE-6796648, TP53 Regulates Transcription of DNA Repair Genes
R-SCE-6807505, RNA polymerase II transcribes snRNA genes
R-SCE-72086, mRNA Capping
R-SCE-73776, RNA Polymerase II Promoter Escape
R-SCE-73779, RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
R-SCE-75953, RNA Polymerase II Transcription Initiation
R-SCE-75955, RNA Polymerase II Transcription Elongation
R-SCE-76042, RNA Polymerase II Transcription Initiation And Promoter Clearance
R-SCE-77075, RNA Pol II CTD phosphorylation and interaction with CE
R-SCE-9018519, Estrogen-dependent gene expression

Miscellaneous databases

EvolutionaryTraceiP08518

Protein Ontology

More...PROi		PR:P08518
RNActiP08518, protein

Family and domain databases

CDDicd00653, RNA_pol_B_RPB2, 1 hit
Gene3Di2.40.270.10, 1 hit
2.40.50.150, 1 hit
3.90.1110.10, 1 hit
InterProiView protein in InterPro
IPR015712, DNA-dir_RNA_pol_su2
IPR007120, DNA-dir_RNAP_su2_dom
IPR037033, DNA-dir_RNAP_su2_hyb_sf
IPR007121, RNA_pol_bsu_CS
IPR007644, RNA_pol_bsu_protrusion
IPR007642, RNA_pol_Rpb2_2
IPR037034, RNA_pol_Rpb2_2_sf
IPR007645, RNA_pol_Rpb2_3
IPR007646, RNA_pol_Rpb2_4
IPR007647, RNA_pol_Rpb2_5
IPR007641, RNA_pol_Rpb2_7
IPR014724, RNA_pol_RPB2_OB-fold
PANTHERiPTHR20856, PTHR20856, 1 hit
PfamiView protein in Pfam
PF04563, RNA_pol_Rpb2_1, 1 hit
PF04561, RNA_pol_Rpb2_2, 1 hit
PF04565, RNA_pol_Rpb2_3, 1 hit
PF04566, RNA_pol_Rpb2_4, 1 hit
PF04567, RNA_pol_Rpb2_5, 1 hit
PF00562, RNA_pol_Rpb2_6, 1 hit
PF04560, RNA_pol_Rpb2_7, 1 hit
PROSITEiView protein in PROSITE
PS01166, RNA_POL_BETA, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRPB2_YEAST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P08518
Secondary accession number(s): D6W2K8, Q12738, Q7Z9Y0
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 1, 1997
Last modified: September 29, 2021
This is version 222 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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