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P08775

- RPB1_MOUSE

UniProt

P08775 - RPB1_MOUSE

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
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 3 (01 Mar 1992)
      Previous versions | rss
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    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
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. transcription from RNA polymerase II promoter Source: UniProtKB

    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

    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.
    GeneTreeiENSGT00730000110946.
    HOGENOMiHOG000222975.
    HOVERGENiHBG004339.
    InParanoidiQ5F298.
    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

    MHGGGPPSGD SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG     50
    RPKLGGLMDP RQGVIERTGR CQTCAGNMTE CPGHFGHIEL AKPVFHVGFL 100
    VKTMKVLRCV CFFCSKLLVD SNNPKIKDIL AKSKGQPKKR LTHVYDLCKG 150
    KNICEGGEEM DNKFGVEQPE GDEDLTKEKG HGGCGRYQPR IRRSGLELYA 200
    EWKHVNEDSQ EKKILLSPER VHEIFKRISD EECFVLGMEP RYARPEWMIV 250
    TVLPVPPLSV RPAVVMQGSA RNQDDLTHKL ADIVKINNQL RRNEQNGAAA 300
    HVIAEDVKLL QFHVATMVDN ELPGLPRAMQ KSGRPLKSLK QRLKGKEGRV 350
    RGNLMGKRVD FSARTVITPD PNLSIDQVGV PRSIAANMTF AEIVTPFNID 400
    RLQELVRRGN SQYPGAKYII RDNGDRIDLR FHPKPSDLHL QTGYKVERHM 450
    CDGDIVIFNR QPTLHKMSMM GHRVRILPWS TFRLNLSVTT PYNADFDGDE 500
    MNLHLPQSLE TRAEIQELAM VPRMIVTPQS NRPVMGIVQD TLTAVRKFTK 550
    RDVFLERGEV MNLLMFLSTW DGKVPQPAIL KPRPLWTGKQ IFSLIIPGHI 600
    NCIRTHSTHP DDEDSGPYKH ISPGDTKVVV ENGELIMGIL CKKSLGTSAG 650
    SLVHISYLEM GHDITRLFYS NIQTVINNWL LIEGHTIGIG DSIADSKTYQ 700
    DIQNTIKKAK QDVIEVIEKA HNNELEPTPG NTLRQTFENQ VNRILNDARD 750
    KTGSSAQKSL SEYNNFKSMV VSGAKGSKIN ISQVIAVVGQ QNVEGKRIPF 800
    GFKHRTLPHF IKDDYGPESR GFVENSYLAG LTPTEFFFHA MGGREGLIDT 850
    AVKTAETGYI QRRLIKSMES VMVKYDATVR NSINQVVQLR YGEDGLAGES 900
    VEFQNLATLK PSNKAFEKKF RFDYTNERAL RRTLQEDLVK DVLSNAHIQN 950
    ELEREFERMR EDREVLRVIF PTGDSKVVLP CNLLRMIWNA QKIFHINPRL 1000
    PSDLHPIKVV EGVKELSKKL VIVNGDDPLS RQAQENATLL FNIHLRSTLC 1050
    SRRMAEEFRL SGEAFDWLLG EIESKFNQAI AHPGEMVGAL AAQSLGEPAT 1100
    QMTLNTFHYA GVSAKNVTLG VPRLKELINI SKKPKTPSLT VFLLGQSARD 1150
    AERAKDILCR LEHTTLRKVT ANTAIYYDPN PQSTVVAEDQ EWVNVYYEMP 1200
    DFDVARISPW LLRVELDRKH MTDRKLTMEQ IAEKINAGFG DDLNCIFNDD 1250
    NAEKLVLRIR IMNSDENKMQ EEEEVVDKMD DDVFLRCIES NMLTDMTLQG 1300
    IEQISKVYMH LPQTDNKKKI IITEDGEFKA LQEWILETDG VSLMRVLSEK 1350
    DVDPVRTTSN DIVEIFTVLG IEAVRKALER ELYHVISFDG SYVNYRHLAL 1400
    LCDTMTCRGH LMAITRHGVN RQDTGPLMKC SFEETVDVLM EAAAHGESDP 1450
    MKGVSENIML GQLAPAGTGC FDLLLDAEKC KYGMEIPTNI PGLGAAGPTG 1500
    MFFGSAPSPM GGISPAMTPW NQGATPAYGA WSPSVGSGMT PGAAGFSPSA 1550
    ASDASGFSPG YSPAWSPTPG SPGSPGPSSP YIPSPGGAMS PSYSPTSPAY 1600
    EPRSPGGYTP QSPSYSPTSP SYSPTSPSYS PTSPNYSPTS PSYSPTSPSY 1650
    SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS 1700
    PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPNYSP 1750
    TSPNYTPTSP SYSPTSPSYS PTSPNYTPTS PNYSPTSPSY SPTSPSYSPT 1800
    SPSYSPSSPR YTPQSPTYTP SSPSYSPSSP SYSPTSPKYT PTSPSYSPSS 1850
    PEYTPASPKY SPTSPKYSPT SPKYSPTSPT YSPTTPKYSP TSPTYSPTSP 1900
    VYTPTSPKYS PTSPTYSPTS PKYSPTSPTY SPTSPKGSTY SPTSPGYSPT 1950
    SPTYSLTSPA ISPDDSDEEN 1970
    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

    MGIi MGI:98086. Polr2a.

    Phylogenomic databases

    eggNOGi COG0086.
    GeneTreei ENSGT00730000110946.
    HOGENOMi HOG000222975.
    HOVERGENi HBG004339.
    InParanoidi Q5F298.
    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

    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 1, 2014
    This is version 151 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