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Entry version 189 (11 Dec 2019)
Sequence version 4 (01 Jun 2001)
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Protein

DNA-directed RNA polymerase II subunit RPB1

Gene

RpII215

Organism
Drosophila melanogaster (Fruit fly)
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>
-Protein inferred from homologyi <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 (By similarity).By similarity

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 <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 bindingi67Zinc 1By similarity1
Metal bindingi70Zinc 1By similarity1
Metal bindingi77Zinc 1By similarity1
Metal bindingi80Zinc 1By similarity1
Metal bindingi107Zinc 2By similarity1
Metal bindingi110Zinc 2By similarity1
Metal bindingi150Zinc 2By similarity1
Metal bindingi176Zinc 2By similarity1
Metal bindingi487Magnesium 1; catalyticBy similarity1
Metal bindingi487Magnesium 2; shared with RPB2By similarity1
Metal bindingi489Magnesium 1; catalyticBy similarity1
Metal bindingi489Magnesium 2; shared with RPB2By similarity1
Metal bindingi491Magnesium 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

GO - Biological processi

  • transcription by RNA polymerase II Source: FlyBase

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DME-112382 Formation of RNA Pol II elongation complex
R-DME-113418 Formation of the Early Elongation Complex
R-DME-5578749 Transcriptional regulation by small RNAs
R-DME-674695 RNA Polymerase II Pre-transcription Events
R-DME-6781823 Formation of TC-NER Pre-Incision Complex
R-DME-6782135 Dual incision in TC-NER
R-DME-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-DME-6796648 TP53 Regulates Transcription of DNA Repair Genes
R-DME-6803529 FGFR2 alternative splicing
R-DME-6807505 RNA polymerase II transcribes snRNA genes
R-DME-72086 mRNA Capping
R-DME-72163 mRNA Splicing - Major Pathway
R-DME-72165 mRNA Splicing - Minor Pathway
R-DME-72203 Processing of Capped Intron-Containing Pre-mRNA
R-DME-73776 RNA Polymerase II Promoter Escape
R-DME-73779 RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
R-DME-75953 RNA Polymerase II Transcription Initiation
R-DME-75955 RNA Polymerase II Transcription Elongation
R-DME-76042 RNA Polymerase II Transcription Initiation And Promoter Clearance
R-DME-77075 RNA Pol II CTD phosphorylation and interaction with CE
R-DME-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 RPB1 (EC:2.7.7.6)
Short name:
RNA polymerase II subunit B1
Alternative name(s):
DNA-directed RNA polymerase III largest subunit
<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:RpII215
ORF Names:CG1554
<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>OrganismiDrosophila melanogaster (Fruit fly)
<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 identifieri7227 [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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
<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
  • UP000000803 <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 X

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0003277 RpII215

<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 & Seán O’Donoghue; Source: COMPARTMENTS

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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000739371 – 1887DNA-directed RNA polymerase II subunit RPB1Add BLAST1887

<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 7 residues 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. The phosphorylation state is believed to result from the balanced action of site-specific CTD kinases and phosphatase, and a 'CTD code' that specifies the position of Pol II within the transcription cycle has been proposed.

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...
PaxDbi
P04052

PRoteomics IDEntifications database

More...
PRIDEi
P04052

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P04052

<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
FBgn0003277 Expressed in 31 organ(s), highest expression level in cleaving embryo

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P04052 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P04052 DM

<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.

By similarity

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
58510, 37 interactors

Database of interacting proteins

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DIPi
DIP-22282N

Protein interaction database and analysis system

More...
IntActi
P04052, 13 interactors

Molecular INTeraction database

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MINTi
P04052

STRING: functional protein association networks

More...
STRINGi
7227.FBpp0073387

<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

3D structure databases

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

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SMRi
P04052

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

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>Repeati1579 – 158517
Repeati1586 – 15922; approximate7
Repeati1598 – 160437
Repeati1605 – 161147
Repeati1631 – 163757
Repeati1638 – 164467
Repeati1671 – 167777
Repeati1678 – 168487
Repeati1685 – 169197
Repeati1692 – 1698107
Repeati1699 – 1705117
Repeati1706 – 1712127
Repeati1713 – 1719137
Repeati1720 – 1726147
Repeati1727 – 1733157
Repeati1740 – 1746167
Repeati1754 – 1760177
Repeati1761 – 1767187
Repeati1777 – 1783197
Repeati1784 – 1790207
Repeati1791 – 1797217
Repeati1798 – 1804227
Repeati1811 – 1817237
Repeati1818 – 182424; approximate7
Repeati1825 – 1831257
Repeati1832 – 1838267
Repeati1839 – 1845277
Repeati1846 – 1852287
Repeati1853 – 1859297
Repeati1860 – 1866307
Repeati1868 – 1874317
Repeati1875 – 1881327

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>Regioni825 – 837Bridging helixAdd BLAST13
Regioni1579 – 1881C-terminal domain (CTD); 32 X 7 AA approximate tandem repeats of Y-[ST]-P-[STNVAPGN]-[STGMA]-[PSTR]-[SNAGCQKTLRIMH]Add BLAST303

<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.Curated

<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

More...
eggNOGi
KOG0260 Eukaryota
COG0086 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00930000151033

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P04052

KEGG Orthology (KO)

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KOi
K03006

Identification of Orthologs from Complete Genome Data

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OMAi
EDGLCGE

Database of Orthologous Groups

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OrthoDBi
591636at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P04052

Family and domain databases

Database of protein disorder

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DisProti
DP01433

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.132.30, 1 hit
1.10.274.100, 1 hit
3.30.1360.140, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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
IPR042102 RNA_pol_Rpb1_3_sf
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

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

More...
PROSITEi
View protein in PROSITE
PS00115 RNA_POL_II_REPEAT, 11 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>. 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.

P04052-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTPTDSKAP LRQVKRVQFG ILSPDEIRRM SVTEGGVQFA ETMEGGRPKL
60 70 80 90 100
GGLMDPRQGV IDRTSRCQTC AGNMTECPGH FGHIDLAKPV FHIGFITKTI
110 120 130 140 150
KILRCVCFYC SKMLVSPHNP KIKEIVMKSR GQPRKRLAYV YDLCKGKTIC
160 170 180 190 200
EGGEDMDLTK ENQQPDPNKK PGHGGCGHYQ PSIRRTGLDL TAEWKHQNED
210 220 230 240 250
SQEKKIVVSA ERVWEILKHI TDEECFILGM DPKYARPDWM IVTVLPVPPL
260 270 280 290 300
AVRPAVVMFG AAKNQDDLTH KLSDIIKANN ELRKNEASGA AAHVIQENIK
310 320 330 340 350
MLQFHVATLV DNDMPGMPRA MQKSGKPLKA IKARLKGKEG RIRGNLMGKR
360 370 380 390 400
VDFSARTVIT PDPNLRIDQV GVPRSIAQNL TFPELVTPFN IDRMQELVRR
410 420 430 440 450
GNSQYPGAKY IVRDNGERID LRFHPKSSDL HLQCGYKVER HLRDDDLVIF
460 470 480 490 500
NRQPTLHKMS MMGHRVKVLP WSTFRMNLSC TSPYNADFDG DEMNLHVPQS
510 520 530 540 550
METRAEVENI HITPRQIITP QANKPVMGIV QDTLTAVRKM TKRDVFITRE
560 570 580 590 600
QVMNLLMFLP TWDAKMPQPC ILKPRPLWTG KQIFSLIIPG NVNMIRTHST
610 620 630 640 650
HPDEEDEGPY KWISPGDTKV MVEHGELIMG ILCKKSLGTS AGSLLHICFL
660 670 680 690 700
ELGHDIAGRF YGNIQTVINN WLLFEGHSIG IGDTIADPQT YNEIQQAIKK
710 720 730 740 750
AKDDVINVIQ KAHNMELEPT PGNTLRQTFE NKVNRILNDA RDKTGGSAKK
760 770 780 790 800
SLTEYNNLKA MVVSGSKGSN INISQVIACV GQQNVEGKRI PYGFRKRTLP
810 820 830 840 850
HFIKDDYGPE SRGFVENSYL AGLTPSEFYF HAMGGREGLI DTAVKTAETG
860 870 880 890 900
YIQRRLIKAM ESVMVNYDGT VRNSVGQLIQ LRYGEDGLCG ELVEFQNMPT
910 920 930 940 950
VKLSNKSFEK RFKFDWSNER LMKKVFTDDV IKEMTDSSEA IQELEAEWDR
960 970 980 990 1000
LVSDRDSLRQ IFPNGESKVV LPCNLQRMIW NVQKIFHINK RLPTDLSPIR
1010 1020 1030 1040 1050
VIKGVKTLLE RCVIVTGNDR ISKQANENAT LLFQCLIRST LCTKYVSEEF
1060 1070 1080 1090 1100
RLSTEAFEWL VGEIETRFQQ AQANPGEMVG ALAAQSLGEP ATQMTLNTFH
1110 1120 1130 1140 1150
FAGVSSKNVT LGVPRLKEII NISKKPKAPS LTVFLTGGAA RDAEKAKNVL
1160 1170 1180 1190 1200
CRLEHTTLRK VTANTAIYYD PDPQRTVISE DQEFVNVYYE MPDFDPTRIS
1210 1220 1230 1240 1250
PWLLRIELDR KRMTDKKLTM EQIAEKINVG FGEDLNCIFN DDNADKLVLR
1260 1270 1280 1290 1300
IRIMNNEENK FQDEDEAVDK MEDDMFLRCI EANMLSDMTL QGIEAIGKVY
1310 1320 1330 1340 1350
MHLPQTDSKK RIVITETGEF KAIGEWLLET DGTSMMKVLS ERDVDPIRTS
1360 1370 1380 1390 1400
SNDICEIFQV LGIEAVRKSV EKEMNAVLQF YGLYVNYRHL ALLCDVMTAK
1410 1420 1430 1440 1450
GHLMAITRHG INRQDTGALM RCSFEETVDV LMDAAAHAET DPMRGVSENI
1460 1470 1480 1490 1500
IMGQLPKMGT GCFDLLLDAE KCRFGIEIPN TLGNSMLGGA AMFIGGGSTP
1510 1520 1530 1540 1550
SMTPPMTPWA NCNTPRYFSP PGHVSAMTPG GPSFSPSAAS DASGMSPSWS
1560 1570 1580 1590 1600
PAHPGSSPSS PGPSMSPYFP ASPSVSPSYS PTSPNYTASS PGGASPNYSP
1610 1620 1630 1640 1650
SSPNYSPTSP LYASPRYAST TPNFNPQSTG YSPSSSGYSP TSPVYSPTVQ
1660 1670 1680 1690 1700
FQSSPSFAGS GSNIYSPGNA YSPSSSNYSP NSPSYSPTSP SYSPSSPSYS
1710 1720 1730 1740 1750
PTSPCYSPTS PSYSPTSPNY TPVTPSYSPT SPNYSASPQY SPASPAYSQT
1760 1770 1780 1790 1800
GVKYSPTSPT YSPPSPSYDG SPGSPQYTPG SPQYSPASPK YSPTSPLYSP
1810 1820 1830 1840 1850
SSPQHSPSNQ YSPTGSTYSA TSPRYSPNMS IYSPSSTKYS PTSPTYTPTA
1860 1870 1880
RNYSPTSPMY SPTAPSHYSP TSPAYSPSSP TFEESED
Length:1,887
Mass (Da):209,168
Last modified:June 1, 2001 - 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:i4EC68C7708A167A3
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 conflicti319 – 324RAMQKS → GYAKV in AAA28863 (PubMed:2992806).Curated6
Sequence conflicti450F → G in AAA28863 (PubMed:2992806).Curated1
Sequence conflicti455 – 458TLHK → RCTT (PubMed:2992806).Curated4
Sequence conflicti463 – 472GHRVKVLPWS → VTGESVASST (PubMed:2992806).Curated10
Sequence conflicti741R → H in AAA28868 (PubMed:2496296).Curated1
Sequence conflicti1485 – 1524SMLGG…PPGHV → I in AAA28827 (PubMed:3122024).CuratedAdd BLAST40
Sequence conflicti1506 – 1508MTP → ELDSA in AAA28868 (PubMed:2496296).Curated3
Sequence conflicti1887D → DVRKGGRG in AAA28868 (PubMed:2496296).Curated1

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
M27431 Genomic DNA Translation: AAA28868.1
AE014298 Genomic DNA Translation: AAF48057.1
M14203 Genomic DNA Translation: AAA28864.1
M11798 Genomic DNA Translation: AAA28863.1
M19537 Genomic DNA Translation: AAA28827.1

Protein sequence database of the Protein Information Resource

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PIRi
S04457 RNFF2L

NCBI Reference Sequences

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RefSeqi
NP_511124.1, NM_078569.3

Genome annotation databases

Ensembl metazoan genome annotation project

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EnsemblMetazoai
FBtr0073542; FBpp0073387; FBgn0003277

Database of genes from NCBI RefSeq genomes

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GeneIDi
32100

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
dme:Dmel_CG1554

<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
M27431 Genomic DNA Translation: AAA28868.1
AE014298 Genomic DNA Translation: AAF48057.1
M14203 Genomic DNA Translation: AAA28864.1
M11798 Genomic DNA Translation: AAA28863.1
M19537 Genomic DNA Translation: AAA28827.1
PIRiS04457 RNFF2L
RefSeqiNP_511124.1, NM_078569.3

3D structure databases

SMRiP04052
ModBaseiSearch...

Protein-protein interaction databases

BioGridi58510, 37 interactors
DIPiDIP-22282N
IntActiP04052, 13 interactors
MINTiP04052
STRINGi7227.FBpp0073387

PTM databases

iPTMnetiP04052

Proteomic databases

PaxDbiP04052
PRIDEiP04052

Protocols and materials databases

ABCD curated depository of sequenced antibodies

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ABCDi
P04052

Genome annotation databases

EnsemblMetazoaiFBtr0073542; FBpp0073387; FBgn0003277
GeneIDi32100
KEGGidme:Dmel_CG1554

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
32100
FlyBaseiFBgn0003277 RpII215

Phylogenomic databases

eggNOGiKOG0260 Eukaryota
COG0086 LUCA
GeneTreeiENSGT00930000151033
InParanoidiP04052
KOiK03006
OMAiEDGLCGE
OrthoDBi591636at2759
PhylomeDBiP04052

Enzyme and pathway databases

ReactomeiR-DME-112382 Formation of RNA Pol II elongation complex
R-DME-113418 Formation of the Early Elongation Complex
R-DME-5578749 Transcriptional regulation by small RNAs
R-DME-674695 RNA Polymerase II Pre-transcription Events
R-DME-6781823 Formation of TC-NER Pre-Incision Complex
R-DME-6782135 Dual incision in TC-NER
R-DME-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-DME-6796648 TP53 Regulates Transcription of DNA Repair Genes
R-DME-6803529 FGFR2 alternative splicing
R-DME-6807505 RNA polymerase II transcribes snRNA genes
R-DME-72086 mRNA Capping
R-DME-72163 mRNA Splicing - Major Pathway
R-DME-72165 mRNA Splicing - Minor Pathway
R-DME-72203 Processing of Capped Intron-Containing Pre-mRNA
R-DME-73776 RNA Polymerase II Promoter Escape
R-DME-73779 RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
R-DME-75953 RNA Polymerase II Transcription Initiation
R-DME-75955 RNA Polymerase II Transcription Elongation
R-DME-76042 RNA Polymerase II Transcription Initiation And Promoter Clearance
R-DME-77075 RNA Pol II CTD phosphorylation and interaction with CE
R-DME-9018519 Estrogen-dependent gene expression

Miscellaneous databases

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

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GenomeRNAii
32100

Protein Ontology

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PROi
PR:P04052

Gene expression databases

BgeeiFBgn0003277 Expressed in 31 organ(s), highest expression level in cleaving embryo
ExpressionAtlasiP04052 baseline and differential
GenevisibleiP04052 DM

Family and domain databases

DisProtiDP01433
Gene3Di1.10.132.30, 1 hit
1.10.274.100, 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
IPR042102 RNA_pol_Rpb1_3_sf
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
SMARTiView protein in SMART
SM00663 RPOLA_N, 1 hit
PROSITEiView protein in PROSITE
PS00115 RNA_POL_II_REPEAT, 11 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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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 nameiRPB1_DROME
<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: P04052
Secondary accession number(s): Q9VYX6
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: June 1, 2001
Last modified: December 11, 2019
This is version 189 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 programDrosophila annotation project

<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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
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