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P08775

- RPB1_MOUSE

UniProt

P08775 - RPB1_MOUSE

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Protein

DNA-directed RNA polymerase II subunit RPB1

Gene

Polr2a

Organism
Mus musculus (Mouse)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi71 – 711Zinc 1By similarity
Metal bindingi74 – 741Zinc 1By similarity
Metal bindingi81 – 811Zinc 1By similarity
Metal bindingi84 – 841Zinc 1By similarity
Metal bindingi111 – 1111Zinc 2By similarity
Metal bindingi114 – 1141Zinc 2By similarity
Metal bindingi154 – 1541Zinc 2By similarity
Metal bindingi184 – 1841Zinc 2By similarity
Metal bindingi495 – 4951Magnesium 1; catalyticBy similarity
Metal bindingi495 – 4951Magnesium 2; shared with RPB2By similarity
Metal bindingi497 – 4971Magnesium 1; catalyticBy similarity
Metal bindingi497 – 4971Magnesium 2; shared with RPB2By similarity
Metal bindingi499 – 4991Magnesium 1; catalyticBy similarity

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. DNA-directed RNA polymerase activity Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. transcription from RNA polymerase II promoter Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Transcription

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_203462. Formation of the Early Elongation Complex.
REACT_213655. Transcription-coupled NER (TC-NER).
REACT_221178. MicroRNA (miRNA) biogenesis.
REACT_223654. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_224562. Dual incision reaction in TC-NER.
REACT_226490. RNA Polymerase II Transcription Elongation.

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
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:98086. Polr2a.

Subcellular locationi

GO - Cellular componenti

  1. DNA-directed RNA polymerase II, core complex Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1859 – 18591K → 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 Publication
Mutagenesisi1866 – 18661K → 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 Publication
Mutagenesisi1873 – 18731K → 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 Publication
Mutagenesisi1887 – 18871K → 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 Publication
Mutagenesisi1908 – 19081K → 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 Publication
Mutagenesisi1922 – 19221K → 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 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19701970DNA-directed RNA polymerase II subunit RPB1PRO_0000073941Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei1810 – 18101Omega-N-methylated arginine; by CARM1By similarity
Modified residuei1843 – 18431PhosphoserineBy similarity
Modified residuei1849 – 18491PhosphoserineBy similarity
Modified residuei1854 – 18541PhosphothreonineBy similarity
Modified residuei1874 – 18741PhosphotyrosineBy similarity
Modified residuei1878 – 18781Phosphoserine
Modified residuei1882 – 18821PhosphoserineBy similarity
Modified residuei1896 – 18961PhosphoserineBy similarity
Modified residuei1899 – 18991PhosphoserineBy similarity
Modified residuei1909 – 19091PhosphotyrosineBy similarity
Modified residuei1913 – 19131PhosphoserineBy similarity
Modified residuei1917 – 19171PhosphoserineBy similarity
Modified residuei1920 – 19201PhosphoserineBy similarity
Modified residuei1923 – 19231Phosphotyrosine
Modified residuei1927 – 19271Phosphoserine
Modified residuei1931 – 19311PhosphoserineBy similarity
Modified residuei1933 – 19331Phosphothreonine
Modified residuei1934 – 19341PhosphoserineBy similarity

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 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 phosphatase, and a 'CTD code' that specifies the position of Pol II within the transcription cycle has been proposed (By similarity).By similarity
Dephosphorylated by the protein phosphatase CTDSP1.By similarity
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 by CARM1. Methylation occurs only when the CTD is hypophosphorylated, and phosphorylation at Ser-1805 and Ser-1808 prevent methylation (in vitro). It is assumed that methylation occurs prior to phosphorylation and transcription initiation. CTD methylation may facilitate the expression of select RNAs (By similarity).By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP08775.
PaxDbiP08775.
PRIDEiP08775.

PTM databases

PhosphoSiteiP08775.

Expressioni

Gene expression databases

BgeeiP08775.
CleanExiMM_POLR2A.
GenevestigatoriP08775.

Interactioni

Subunit structurei

Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits. The phosphorylated C-terminal domain interacts with FNBP3 and SYNCRIP. Interacts with SAFB/SAFB1. Interacts with CCNL1, CCNL2 and SFRS19. 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. Hyperphosphorylated form on tandem 7 residues repeats specifically interacts with SETD2. Interacts with PAF1. Interacts (via C-terminus) with CMTR1 and CTDSP1. Interacts with MYO1C. Interacts (via C-terminus) with SCAF8. Interacts via the phosphorylated C-terminal domain with WDR82 and with SETD1A and SETD1B only in the presence of WDR82. Interacts with ATF7IP. When phosphorylated at 'Ser-5', interacts with MEN1; the unphosphorylated form, or phosphorylated at 'Ser-2' does not interact. Interacts with DDX5. When phosphorylated at 'Ser-2', interacts with SUPT6H (via SH2 domain). The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active).5 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi202996. 24 interactions.
DIPiDIP-46369N.
IntActiP08775. 17 interactions.
MINTiMINT-4133043.

Structurei

3D structure databases

DisProtiDP00181.
ProteinModelPortaliP08775.
SMRiP08775. Positions 16-896, 1072-1475.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1593 – 159971
Repeati1600 – 160672; approximate
Repeati1608 – 161473
Repeati1615 – 162174
Repeati1622 – 162875
Repeati1629 – 163576
Repeati1636 – 164277
Repeati1643 – 164978
Repeati1650 – 165679
Repeati1657 – 1663710
Repeati1664 – 1670711
Repeati1671 – 1677712
Repeati1678 – 1684713
Repeati1685 – 1691714
Repeati1692 – 1698715
Repeati1699 – 1705716
Repeati1706 – 1712717
Repeati1713 – 1719718
Repeati1720 – 1726719
Repeati1727 – 1733720
Repeati1734 – 1740721
Repeati1741 – 1747722
Repeati1748 – 1754723
Repeati1755 – 1761724
Repeati1762 – 1768725
Repeati1769 – 1775726
Repeati1776 – 1782727
Repeati1783 – 1789728
Repeati1790 – 1796729
Repeati1797 – 1803730
Repeati1804 – 1810731
Repeati1811 – 1817732
Repeati1818 – 1824733
Repeati1825 – 1831734
Repeati1832 – 1838735
Repeati1839 – 1845736
Repeati1846 – 1852737
Repeati1853 – 1859738
Repeati1860 – 1866739
Repeati1867 – 1873740
Repeati1874 – 1880741
Repeati1881 – 1887742
Repeati1888 – 1894743
Repeati1895 – 1901744
Repeati1902 – 1908745
Repeati1909 – 1915746
Repeati1916 – 1922747
Repeati1923 – 1929748
Repeati1930 – 1936749
Repeati1940 – 1946750
Repeati1947 – 1953751; approximate
Repeati1954 – 1960752; approximate

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni833 – 84513Bridging helixAdd
BLAST
Regioni1593 – 196036852 X 7 AA approximate tandem repeats of Y-[ST]-P-[STQ]-[ST]-P-[SRNTEVKGN]Add
BLAST

Sequence similaritiesi

Belongs to the RNA polymerase beta' chain family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0086.
GeneTreeiENSGT00760000119460.
HOGENOMiHOG000222975.
HOVERGENiHBG004339.
InParanoidiP08775.
OMAiIVFNRQP.
OrthoDBiEOG7K0ZB8.
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. 25 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1498 – 14981P → R in AAA40071. (PubMed:3038894)Curated
Sequence conflicti1499 – 153638Missing in AAA40071. (PubMed:3038894)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
ENSMUST00000071213; ENSMUSP00000071200; ENSMUSG00000005198.
GeneIDi20020.
UCSCiuc007jrj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12130 , M14101 Genomic DNA. Translation: AAA40071.1 .
AL603707 Genomic DNA. Translation: CAI51953.1 .
CCDSi CCDS70217.1.
PIRi A28490.
RefSeqi NP_001277997.1. NM_001291068.1.
UniGenei Mm.16533.

3D structure databases

DisProti DP00181.
ProteinModelPortali P08775.
SMRi P08775. Positions 16-896, 1072-1475.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202996. 24 interactions.
DIPi DIP-46369N.
IntActi P08775. 17 interactions.
MINTi MINT-4133043.

PTM databases

PhosphoSitei P08775.

Proteomic databases

MaxQBi P08775.
PaxDbi P08775.
PRIDEi P08775.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000058470 ; ENSMUSP00000050771 ; ENSMUSG00000005198 .
ENSMUST00000071213 ; ENSMUSP00000071200 ; ENSMUSG00000005198 .
GeneIDi 20020.
UCSCi uc007jrj.1. mouse.

Organism-specific databases

CTDi 5430.
MGIi MGI:98086. Polr2a.

Phylogenomic databases

eggNOGi COG0086.
GeneTreei ENSGT00760000119460.
HOGENOMi HOG000222975.
HOVERGENi HBG004339.
InParanoidi P08775.
OMAi IVFNRQP.
OrthoDBi EOG7K0ZB8.
PhylomeDBi P08775.
TreeFami TF103036.

Enzyme and pathway databases

Reactomei REACT_203462. Formation of the Early Elongation Complex.
REACT_213655. Transcription-coupled NER (TC-NER).
REACT_221178. MicroRNA (miRNA) biogenesis.
REACT_223654. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_224562. Dual incision reaction in TC-NER.
REACT_226490. RNA Polymerase II Transcription Elongation.

Miscellaneous databases

ChiTaRSi POLR2A. mouse.
NextBioi 297535.
PROi P08775.
SOURCEi Search...

Gene expression databases

Bgeei P08775.
CleanExi MM_POLR2A.
Genevestigatori P08775.

Family and domain databases

InterProi IPR000722. RNA_pol_asu.
IPR000684. RNA_pol_II_repeat_euk.
IPR006592. RNA_pol_N.
IPR007080. RNA_pol_Rpb1_1.
IPR007066. RNA_pol_Rpb1_3.
IPR007083. RNA_pol_Rpb1_4.
IPR007081. RNA_pol_Rpb1_5.
IPR007075. RNA_pol_Rpb1_6.
IPR007073. RNA_pol_Rpb1_7.
[Graphical view ]
Pfami PF04997. RNA_pol_Rpb1_1. 1 hit.
PF00623. RNA_pol_Rpb1_2. 1 hit.
PF04983. RNA_pol_Rpb1_3. 1 hit.
PF05000. RNA_pol_Rpb1_4. 1 hit.
PF04998. RNA_pol_Rpb1_5. 1 hit.
PF04992. RNA_pol_Rpb1_6. 1 hit.
PF04990. RNA_pol_Rpb1_7. 1 hit.
PF05001. RNA_pol_Rpb1_R. 25 hits.
[Graphical view ]
SMARTi SM00663. RPOLA_N. 1 hit.
[Graphical view ]
PROSITEi PS00115. RNA_POL_II_REPEAT. 42 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of the mouse genomic locus encoding the largest subunit of RNA polymerase II."
    Ahearn J.M. Jr., Bartolomei M.S., West M.L., Cisek L.J., Corden J.L.
    J. Biol. Chem. 262:10695-10705(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "A unique structure at the carboxyl terminus of the largest subunit of eukaryotic RNA polymerase II."
    Corden J.L., Cadena D.L., Ahearn J.M. Jr., Dahmus M.E.
    Proc. Natl. Acad. Sci. U.S.A. 82:7934-7938(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1587-1970.
  4. "Complete sequence of the human RNA polymerase II largest subunit."
    Wintzerith M., Acker J., Vicaire S., Vigneron M., Kedinger C.
    Nucleic Acids Res. 20:910-910(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION, PRESENCE OF AN ADDITIONAL EXON.
  5. "The C-terminal domain of the largest subunit of RNA polymerase II interacts with a novel set of serine/arginine-rich proteins."
    Yuryev A., Patturajan M., Litingtung Y., Joshi R.V., Gentile C., Gebara M., Corden J.L.
    Proc. Natl. Acad. Sci. U.S.A. 93:6975-6980(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCAF8.
  6. Cited for: INTERACTION WITH MYO1C.
  7. "Wwp2-mediated ubiquitination of the RNA polymerase II large subunit in mouse embryonic pluripotent stem cells."
    Li H., Zhang Z., Wang B., Zhang J., Zhao Y., Jin Y.
    Mol. Cell. Biol. 27:5296-5305(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-1859; LYS-1866; LYS-1873; LYS-1887; LYS-1908 AND LYS-1922, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH WWP2, MUTAGENESIS OF LYS-1859; LYS-1866; LYS-1873; LYS-1887; LYS-1908 AND LYS-1922.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "The Iws1:Spt6:CTD complex controls cotranscriptional mRNA biosynthesis and HYPB/Setd2-mediated histone H3K36 methylation."
    Yoh S.M., Lucas J.S., Jones K.A.
    Genes Dev. 22:3422-3434(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUPT6H.
  10. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Feedback regulation of transcriptional termination by the mammalian circadian clock PERIOD complex."
    Padmanabhan K., Robles M.S., Westerling T., Weitz C.J.
    Science 337:599-602(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A LARGE PER COMPLEX.

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: October 29, 2014
This is version 152 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

External Data

Dasty 3