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Protein

DNA-directed RNA polymerase II subunit RPB1

Gene

Polr2a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi71Zinc 1By similarity1
Metal bindingi74Zinc 1By similarity1
Metal bindingi81Zinc 1By similarity1
Metal bindingi84Zinc 1By similarity1
Metal bindingi111Zinc 2By similarity1
Metal bindingi114Zinc 2By similarity1
Metal bindingi154Zinc 2By similarity1
Metal bindingi184Zinc 2By similarity1
Metal bindingi495Magnesium 1; catalyticBy similarity1
Metal bindingi495Magnesium 2; shared with RPB2By similarity1
Metal bindingi497Magnesium 1; catalyticBy similarity1
Metal bindingi497Magnesium 2; shared with RPB2By similarity1
Metal bindingi499Magnesium 1; catalyticBy similarity1

GO - Molecular functioni

  • core promoter binding Source: BHF-UCL
  • DNA binding Source: MGI
  • DNA-directed RNA polymerase activity Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: MGI
  • ubiquitin protein ligase binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Transcription

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-112382. Formation of RNA Pol II elongation complex.
R-MMU-112387. Elongation arrest and recovery.
R-MMU-113418. Formation of the Early Elongation Complex.
R-MMU-5578749. Transcriptional regulation by small RNAs.
R-MMU-5601884. PIWI-interacting RNA (piRNA) biogenesis.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-MMU-674695. RNA Polymerase II Pre-transcription Events.
R-MMU-6781823. Formation of TC-NER Pre-Incision Complex.
R-MMU-6782135. Dual incision in TC-NER.
R-MMU-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-MMU-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-MMU-6803529. FGFR2 alternative splicing.
R-MMU-6807505. RNA polymerase II transcribes snRNA genes.
R-MMU-72086. mRNA Capping.
R-MMU-72163. mRNA Splicing - Major Pathway.
R-MMU-72165. mRNA Splicing - Minor Pathway.
R-MMU-72203. Processing of Capped Intron-Containing Pre-mRNA.
R-MMU-73776. RNA Polymerase II Promoter Escape.
R-MMU-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-MMU-75953. RNA Polymerase II Transcription Initiation.
R-MMU-75955. RNA Polymerase II Transcription Elongation.
R-MMU-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-MMU-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase II subunit RPB1 (EC:2.7.7.6)
Short name:
RNA polymerase II subunit B1
Alternative name(s):
DNA-directed RNA polymerase II subunit A
DNA-directed RNA polymerase III largest subunit
Gene namesi
Name:Polr2a
Synonyms:Rpii215, Rpo2-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:98086. Polr2a.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1859K → R: Loss of ubiquitination, no effect on interaction with WWP2; when associated with R-1866; R-1873; R-1887; R-1908 and R-1922. 1 Publication1
Mutagenesisi1866K → R: Loss of ubiquitination, no effect on interaction with WWP2; when associated with R-1859; R-1873; R-1887; R-1908 and R-1922. 1 Publication1
Mutagenesisi1873K → R: Loss of ubiquitination, no effect on interaction with WWP2; when associated with R-1859; R-1866; R-1887; R-1908 and R-1922. 1 Publication1
Mutagenesisi1887K → R: Loss of ubiquitination, no effect on interaction with WWP2; when associated with R-1859; R-1866; R-1873; R-1908 and R-1922. 1 Publication1
Mutagenesisi1908K → R: Loss of ubiquitination, no effect on interaction with WWP2; when associated with R-1859; R-1866; R-1873; R-1887 and R-1922. 1 Publication1
Mutagenesisi1922K → R: Loss of ubiquitination, no effect on interaction with WWP2; when associated with R-1859; R-1866; R-1873; R-1887 and R-1908. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000739411 – 1970DNA-directed RNA polymerase II subunit RPB1Add BLAST1970

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei27PhosphoserineBy similarity1
Modified residuei217PhosphoserineBy similarity1
Modified residuei1603Omega-N-methylated arginine; by CARM1; in vitroBy similarity1
Modified residuei1810Asymmetric dimethylarginine; alternate; by CARM1By similarity1
Modified residuei1810Symmetric dimethylarginine; alternate; by PRMT5By similarity1
Modified residuei1843PhosphoserineBy similarity1
Modified residuei1847PhosphoserineCombined sources1
Modified residuei1849PhosphoserineCombined sources1
Modified residuei1850PhosphoserineBy similarity1
Modified residuei1854PhosphothreonineCombined sources1
Modified residuei1857PhosphoserineCombined sources1
Modified residuei1864PhosphoserineBy similarity1
Modified residuei1868PhosphoserineBy similarity1
Modified residuei1874PhosphotyrosineCombined sources1
Modified residuei1878PhosphoserineCombined sources1
Modified residuei1882PhosphoserineCombined sources1
Modified residuei1885PhosphothreonineBy similarity1
Modified residuei1894PhosphothreonineCombined sources1
Modified residuei1896PhosphoserineBy similarity1
Modified residuei1899PhosphoserineCombined sources1
Modified residuei1906PhosphoserineBy similarity1
Modified residuei1909PhosphotyrosineCombined sources1
Modified residuei1912PhosphothreonineCombined sources1
Modified residuei1913PhosphoserineCombined sources1
Modified residuei1917PhosphoserineCombined sources1
Modified residuei1920PhosphoserineCombined sources1
Modified residuei1923PhosphotyrosineCombined sources1
Modified residuei1926PhosphothreonineCombined sources1
Modified residuei1927PhosphoserineCombined sources1
Modified residuei1931PhosphoserineCombined sources1
Modified residuei1934PhosphoserineCombined sources1

Post-translational modificationi

The tandem heptapeptide repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat and is mediated, at least, by CDK7 and CDK9. CDK7 phosphorylation of POLR2A associated with DNA promotes transcription initiation by triggering dissociation from DNA. Phosphorylation also takes place at 'Ser-7' of the heptapeptide repeat, which is required for efficient transcription of snRNA genes and processing of the transcripts. The phosphorylation state is believed to result from the balanced action of site-specific CTD kinases and phosphatases, and a 'CTD code' that specifies the position of Pol II within the transcription cycle has been proposed. Dephosphorylated by the protein phosphatase CTDSP1.By similarity
Among tandem heptapeptide repeats of the C-terminal domain (CTD) some do not match the Y-S-P-T-S-P-S consensus, the seventh serine residue 'Ser-7' being replaced by a lysine. 'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated and dimethylated. EP300 is one of the enzyme able to acetylate 'Lys-7'. Acetylation at 'Lys-7' of non-consensus heptapeptide repeats is associated with 'Ser-2' phosphorylation and active transcription. It may regulate initiation or early elongation steps of transcription specially for inducible genes.2 Publications
Following UV treatment, the elongating form of RNA polymerase II (RNA pol IIo) is ubiquitinated UV damage sites without leading to degradation: ubiquitination is facilitated by KIAA1530/UVSSA and promotes RNA pol IIo backtracking to allow access to the nucleotide excision repair machinery (By similarity.) Ubiquitinated by WWP2 leading to proteasomal degradation.1 Publication
Methylated at Arg-1810 prior to transcription initiation when the CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808 preventing this methylation. Symmetrically or asymmetrically dimethylated at Arg-1810 by PRMT5 and CARM1 respectively. Symmetric or asymmetric dimethylation modulates interactions with CTD-binding proteins like SMN1/SMN2 and TDRD3. SMN1/SMN2 interacts preferentially with the symmetrically dimethylated form while TDRD3 interacts with the asymmetric form. Through the recruitment of SMN1/SMN2, symmetric dimethylation is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. CTD dimethylation may also facilitate the expression of select RNAs. Among tandem heptapeptide repeats of the C-terminal domain (CTD) some do not match the Y-S-P-T-S-P-S consensus, the seventh serine residue 'Ser-7' being replaced by a lysine. 'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated and dimethylated. Methylation occurs in the earliest transcription stages and precedes or is concomitant to 'Ser-5' and 'Ser-7' phosphorylation.By similarity1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP08775.
MaxQBiP08775.
PaxDbiP08775.
PRIDEiP08775.

PTM databases

iPTMnetiP08775.
PhosphoSitePlusiP08775.

Expressioni

Gene expression databases

BgeeiENSMUSG00000005198.
CleanExiMM_POLR2A.
ExpressionAtlasiP08775. baseline and differential.
GenevisibleiP08775. MM.

Interactioni

Subunit structurei

Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits. Component of a complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active). Interacts (via the C-terminal domain (CTD)) with U2AF2; recruits PRPF19 and the Prp19 complex to the pre-mRNA and may couple transcription to pre-mRNA splicing. Interacts (via the C-terminal domain (CTD)) with SMN1/SMN2; recruits SMN1/SMN2 to RNA Pol II elongation complexes. Interacts via the phosphorylated C-terminal domain with WDR82 and with SETD1A and SETD1B only in the presence of WDR82. When phosphorylated at 'Ser-5', interacts with MEN1; the unphosphorylated form, or phosphorylated at 'Ser-2' does not interact. When phosphorylated at 'Ser-2', interacts with SUPT6H (via SH2 domain). Interacts with RECQL5 and TCEA1; binding of RECQL5 prevents TCEA1 binding. The phosphorylated C-terminal domain interacts with FNBP3 and SYNCRIP. Interacts with ATF7IP. Interacts with DDX5. Interacts with WWP2. Interacts with SETX. Interacts (phosphorylated) with PIH1D1. Interacts (via the C-terminal domain (CTD)) with TDRD3. Interacts with PRMT5. Interacts with XRN2. Interacts with SAFB/SAFB1. Interacts with CCNL1. Interacts with CCNL2, MYO1C, PAF1 and SFRS19. Interacts (via C-terminus) with CMTR1, CTDSP1 and SCAF8. Interacts (via the C-terminal domain (CTD)) with CCNT2 (By similarity).By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Srsf1Q6PDM22EBI-2549849,EBI-2550360
Srsf2Q620932EBI-2549849,EBI-2550402

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202996. 26 interactors.
DIPiDIP-46369N.
IntActiP08775. 17 interactors.
MINTiMINT-4133043.
STRINGi10090.ENSMUSP00000071200.

Structurei

3D structure databases

DisProtiDP00181.
ProteinModelPortaliP08775.
SMRiP08775.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati1593 – 159917
Repeati1600 – 16062; approximate7
Repeati1608 – 161437
Repeati1615 – 162147
Repeati1622 – 162857
Repeati1629 – 163567
Repeati1636 – 164277
Repeati1643 – 164987
Repeati1650 – 165697
Repeati1657 – 1663107
Repeati1664 – 1670117
Repeati1671 – 1677127
Repeati1678 – 1684137
Repeati1685 – 1691147
Repeati1692 – 1698157
Repeati1699 – 1705167
Repeati1706 – 1712177
Repeati1713 – 1719187
Repeati1720 – 1726197
Repeati1727 – 1733207
Repeati1734 – 1740217
Repeati1741 – 1747227
Repeati1748 – 1754237
Repeati1755 – 1761247
Repeati1762 – 1768257
Repeati1769 – 1775267
Repeati1776 – 1782277
Repeati1783 – 1789287
Repeati1790 – 1796297
Repeati1797 – 1803307
Repeati1804 – 1810317
Repeati1811 – 1817327
Repeati1818 – 1824337
Repeati1825 – 1831347
Repeati1832 – 1838357
Repeati1839 – 1845367
Repeati1846 – 1852377
Repeati1853 – 1859387
Repeati1860 – 1866397
Repeati1867 – 1873407
Repeati1874 – 1880417
Repeati1881 – 1887427
Repeati1888 – 1894437
Repeati1895 – 1901447
Repeati1902 – 1908457
Repeati1909 – 1915467
Repeati1916 – 1922477
Repeati1923 – 1929487
Repeati1930 – 1936497
Repeati1940 – 1946507
Repeati1947 – 195351; approximate7
Repeati1954 – 196052; approximate7

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni833 – 845Bridging helixAdd BLAST13
Regioni1593 – 1960C-terminal domain (CTD); 52 X 7 AA approximate tandem repeats of Y-[ST]-P-[STQ]-[ST]-P-[SRNTEVKGN]Add BLAST368

Domaini

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

Sequence similaritiesi

Belongs to the RNA polymerase beta' chain family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0260. Eukaryota.
COG0086. LUCA.
GeneTreeiENSGT00860000133919.
HOGENOMiHOG000222975.
HOVERGENiHBG004339.
InParanoidiP08775.
KOiK03006.
OMAiDEDNGPY.
OrthoDBiEOG091G00CH.
PhylomeDBiP08775.
TreeFamiTF103036.

Family and domain databases

InterProiIPR000722. RNA_pol_asu.
IPR000684. RNA_pol_II_repeat_euk.
IPR006592. RNA_pol_N.
IPR007080. RNA_pol_Rpb1_1.
IPR007066. RNA_pol_Rpb1_3.
IPR007083. RNA_pol_Rpb1_4.
IPR007081. RNA_pol_Rpb1_5.
IPR007075. RNA_pol_Rpb1_6.
IPR007073. RNA_pol_Rpb1_7.
[Graphical view]
PfamiPF04997. RNA_pol_Rpb1_1. 1 hit.
PF00623. RNA_pol_Rpb1_2. 1 hit.
PF04983. RNA_pol_Rpb1_3. 1 hit.
PF05000. RNA_pol_Rpb1_4. 1 hit.
PF04998. RNA_pol_Rpb1_5. 1 hit.
PF04992. RNA_pol_Rpb1_6. 1 hit.
PF04990. RNA_pol_Rpb1_7. 1 hit.
PF05001. RNA_pol_Rpb1_R. 24 hits.
[Graphical view]
SMARTiSM00663. RPOLA_N. 1 hit.
[Graphical view]
PROSITEiPS00115. RNA_POL_II_REPEAT. 42 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08775-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHGGGPPSGD SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG
60 70 80 90 100
RPKLGGLMDP RQGVIERTGR CQTCAGNMTE CPGHFGHIEL AKPVFHVGFL
110 120 130 140 150
VKTMKVLRCV CFFCSKLLVD SNNPKIKDIL AKSKGQPKKR LTHVYDLCKG
160 170 180 190 200
KNICEGGEEM DNKFGVEQPE GDEDLTKEKG HGGCGRYQPR IRRSGLELYA
210 220 230 240 250
EWKHVNEDSQ EKKILLSPER VHEIFKRISD EECFVLGMEP RYARPEWMIV
260 270 280 290 300
TVLPVPPLSV RPAVVMQGSA RNQDDLTHKL ADIVKINNQL RRNEQNGAAA
310 320 330 340 350
HVIAEDVKLL QFHVATMVDN ELPGLPRAMQ KSGRPLKSLK QRLKGKEGRV
360 370 380 390 400
RGNLMGKRVD FSARTVITPD PNLSIDQVGV PRSIAANMTF AEIVTPFNID
410 420 430 440 450
RLQELVRRGN SQYPGAKYII RDNGDRIDLR FHPKPSDLHL QTGYKVERHM
460 470 480 490 500
CDGDIVIFNR QPTLHKMSMM GHRVRILPWS TFRLNLSVTT PYNADFDGDE
510 520 530 540 550
MNLHLPQSLE TRAEIQELAM VPRMIVTPQS NRPVMGIVQD TLTAVRKFTK
560 570 580 590 600
RDVFLERGEV MNLLMFLSTW DGKVPQPAIL KPRPLWTGKQ IFSLIIPGHI
610 620 630 640 650
NCIRTHSTHP DDEDSGPYKH ISPGDTKVVV ENGELIMGIL CKKSLGTSAG
660 670 680 690 700
SLVHISYLEM GHDITRLFYS NIQTVINNWL LIEGHTIGIG DSIADSKTYQ
710 720 730 740 750
DIQNTIKKAK QDVIEVIEKA HNNELEPTPG NTLRQTFENQ VNRILNDARD
760 770 780 790 800
KTGSSAQKSL SEYNNFKSMV VSGAKGSKIN ISQVIAVVGQ QNVEGKRIPF
810 820 830 840 850
GFKHRTLPHF IKDDYGPESR GFVENSYLAG LTPTEFFFHA MGGREGLIDT
860 870 880 890 900
AVKTAETGYI QRRLIKSMES VMVKYDATVR NSINQVVQLR YGEDGLAGES
910 920 930 940 950
VEFQNLATLK PSNKAFEKKF RFDYTNERAL RRTLQEDLVK DVLSNAHIQN
960 970 980 990 1000
ELEREFERMR EDREVLRVIF PTGDSKVVLP CNLLRMIWNA QKIFHINPRL
1010 1020 1030 1040 1050
PSDLHPIKVV EGVKELSKKL VIVNGDDPLS RQAQENATLL FNIHLRSTLC
1060 1070 1080 1090 1100
SRRMAEEFRL SGEAFDWLLG EIESKFNQAI AHPGEMVGAL AAQSLGEPAT
1110 1120 1130 1140 1150
QMTLNTFHYA GVSAKNVTLG VPRLKELINI SKKPKTPSLT VFLLGQSARD
1160 1170 1180 1190 1200
AERAKDILCR LEHTTLRKVT ANTAIYYDPN PQSTVVAEDQ EWVNVYYEMP
1210 1220 1230 1240 1250
DFDVARISPW LLRVELDRKH MTDRKLTMEQ IAEKINAGFG DDLNCIFNDD
1260 1270 1280 1290 1300
NAEKLVLRIR IMNSDENKMQ EEEEVVDKMD DDVFLRCIES NMLTDMTLQG
1310 1320 1330 1340 1350
IEQISKVYMH LPQTDNKKKI IITEDGEFKA LQEWILETDG VSLMRVLSEK
1360 1370 1380 1390 1400
DVDPVRTTSN DIVEIFTVLG IEAVRKALER ELYHVISFDG SYVNYRHLAL
1410 1420 1430 1440 1450
LCDTMTCRGH LMAITRHGVN RQDTGPLMKC SFEETVDVLM EAAAHGESDP
1460 1470 1480 1490 1500
MKGVSENIML GQLAPAGTGC FDLLLDAEKC KYGMEIPTNI PGLGAAGPTG
1510 1520 1530 1540 1550
MFFGSAPSPM GGISPAMTPW NQGATPAYGA WSPSVGSGMT PGAAGFSPSA
1560 1570 1580 1590 1600
ASDASGFSPG YSPAWSPTPG SPGSPGPSSP YIPSPGGAMS PSYSPTSPAY
1610 1620 1630 1640 1650
EPRSPGGYTP QSPSYSPTSP SYSPTSPSYS PTSPNYSPTS PSYSPTSPSY
1660 1670 1680 1690 1700
SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS
1710 1720 1730 1740 1750
PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPNYSP
1760 1770 1780 1790 1800
TSPNYTPTSP SYSPTSPSYS PTSPNYTPTS PNYSPTSPSY SPTSPSYSPT
1810 1820 1830 1840 1850
SPSYSPSSPR YTPQSPTYTP SSPSYSPSSP SYSPTSPKYT PTSPSYSPSS
1860 1870 1880 1890 1900
PEYTPASPKY SPTSPKYSPT SPKYSPTSPT YSPTTPKYSP TSPTYSPTSP
1910 1920 1930 1940 1950
VYTPTSPKYS PTSPTYSPTS PKYSPTSPTY SPTSPKGSTY SPTSPGYSPT
1960 1970
SPTYSLTSPA ISPDDSDEEN
Length:1,970
Mass (Da):217,176
Last modified:March 1, 1992 - v3
Checksum:i7D76F38FD92A657E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1498P → R in AAA40071 (PubMed:3038894).Curated1
Sequence conflicti1499 – 1536Missing in AAA40071 (PubMed:3038894).CuratedAdd BLAST38

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12130, M14101 Genomic DNA. Translation: AAA40071.1.
AL603707 Genomic DNA. Translation: CAI51953.1.
CCDSiCCDS70217.1.
PIRiA28490.
RefSeqiNP_001277997.1. NM_001291068.1.
UniGeneiMm.16533.

Genome annotation databases

EnsembliENSMUST00000058470; ENSMUSP00000050771; ENSMUSG00000005198.
GeneIDi20020.
KEGGimmu:20020.
UCSCiuc007jrk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12130, M14101 Genomic DNA. Translation: AAA40071.1.
AL603707 Genomic DNA. Translation: CAI51953.1.
CCDSiCCDS70217.1.
PIRiA28490.
RefSeqiNP_001277997.1. NM_001291068.1.
UniGeneiMm.16533.

3D structure databases

DisProtiDP00181.
ProteinModelPortaliP08775.
SMRiP08775.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202996. 26 interactors.
DIPiDIP-46369N.
IntActiP08775. 17 interactors.
MINTiMINT-4133043.
STRINGi10090.ENSMUSP00000071200.

PTM databases

iPTMnetiP08775.
PhosphoSitePlusiP08775.

Proteomic databases

EPDiP08775.
MaxQBiP08775.
PaxDbiP08775.
PRIDEiP08775.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000058470; ENSMUSP00000050771; ENSMUSG00000005198.
GeneIDi20020.
KEGGimmu:20020.
UCSCiuc007jrk.2. mouse.

Organism-specific databases

CTDi5430.
MGIiMGI:98086. Polr2a.

Phylogenomic databases

eggNOGiKOG0260. Eukaryota.
COG0086. LUCA.
GeneTreeiENSGT00860000133919.
HOGENOMiHOG000222975.
HOVERGENiHBG004339.
InParanoidiP08775.
KOiK03006.
OMAiDEDNGPY.
OrthoDBiEOG091G00CH.
PhylomeDBiP08775.
TreeFamiTF103036.

Enzyme and pathway databases

ReactomeiR-MMU-112382. Formation of RNA Pol II elongation complex.
R-MMU-112387. Elongation arrest and recovery.
R-MMU-113418. Formation of the Early Elongation Complex.
R-MMU-5578749. Transcriptional regulation by small RNAs.
R-MMU-5601884. PIWI-interacting RNA (piRNA) biogenesis.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-MMU-674695. RNA Polymerase II Pre-transcription Events.
R-MMU-6781823. Formation of TC-NER Pre-Incision Complex.
R-MMU-6782135. Dual incision in TC-NER.
R-MMU-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-MMU-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-MMU-6803529. FGFR2 alternative splicing.
R-MMU-6807505. RNA polymerase II transcribes snRNA genes.
R-MMU-72086. mRNA Capping.
R-MMU-72163. mRNA Splicing - Major Pathway.
R-MMU-72165. mRNA Splicing - Minor Pathway.
R-MMU-72203. Processing of Capped Intron-Containing Pre-mRNA.
R-MMU-73776. RNA Polymerase II Promoter Escape.
R-MMU-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-MMU-75953. RNA Polymerase II Transcription Initiation.
R-MMU-75955. RNA Polymerase II Transcription Elongation.
R-MMU-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-MMU-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Miscellaneous databases

ChiTaRSiPolr2a. mouse.
PROiP08775.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000005198.
CleanExiMM_POLR2A.
ExpressionAtlasiP08775. baseline and differential.
GenevisibleiP08775. MM.

Family and domain databases

InterProiIPR000722. RNA_pol_asu.
IPR000684. RNA_pol_II_repeat_euk.
IPR006592. RNA_pol_N.
IPR007080. RNA_pol_Rpb1_1.
IPR007066. RNA_pol_Rpb1_3.
IPR007083. RNA_pol_Rpb1_4.
IPR007081. RNA_pol_Rpb1_5.
IPR007075. RNA_pol_Rpb1_6.
IPR007073. RNA_pol_Rpb1_7.
[Graphical view]
PfamiPF04997. RNA_pol_Rpb1_1. 1 hit.
PF00623. RNA_pol_Rpb1_2. 1 hit.
PF04983. RNA_pol_Rpb1_3. 1 hit.
PF05000. RNA_pol_Rpb1_4. 1 hit.
PF04998. RNA_pol_Rpb1_5. 1 hit.
PF04992. RNA_pol_Rpb1_6. 1 hit.
PF04990. RNA_pol_Rpb1_7. 1 hit.
PF05001. RNA_pol_Rpb1_R. 24 hits.
[Graphical view]
SMARTiSM00663. RPOLA_N. 1 hit.
[Graphical view]
PROSITEiPS00115. RNA_POL_II_REPEAT. 42 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRPB1_MOUSE
AccessioniPrimary (citable) accession number: P08775
Secondary accession number(s): Q5F298
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: March 1, 1992
Last modified: November 30, 2016
This is version 175 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.