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P24928

- RPB1_HUMAN

UniProt

P24928 - RPB1_HUMAN

Protein

DNA-directed RNA polymerase II subunit RPB1

Gene

POLR2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 2 (15 Dec 2009)
      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. Acts as an RNA-dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, acting both as a replicate and transcriptase for the viral RNA circular genome.4 Publications

    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: UniProtKB
    2. DNA-directed RNA polymerase activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. RNA-directed RNA polymerase activity Source: UniProtKB-KW
    7. ubiquitin protein ligase binding Source: BHF-UCL

    GO - Biological processi

    1. 7-methylguanosine mRNA capping Source: Reactome
    2. DNA repair Source: Reactome
    3. gene expression Source: Reactome
    4. mRNA splicing, via spliceosome Source: Reactome
    5. nucleotide-excision repair Source: Reactome
    6. positive regulation of viral transcription Source: Reactome
    7. regulation of transcription, DNA-templated Source: UniProtKB
    8. RNA splicing Source: Reactome
    9. transcription-coupled nucleotide-excision repair Source: Reactome
    10. transcription elongation from RNA polymerase II promoter Source: Reactome
    11. transcription from RNA polymerase II promoter Source: UniProtKB
    12. transcription initiation from RNA polymerase II promoter Source: Reactome
    13. viral process Source: Reactome

    Keywords - Molecular functioni

    Nucleotidyltransferase, RNA-directed RNA polymerase, Transferase

    Keywords - Biological processi

    Transcription

    Keywords - Ligandi

    DNA-binding, Magnesium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_12417. MicroRNA (miRNA) biogenesis.
    REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
    REACT_1470. mRNA Capping.
    REACT_1628. Transcription-coupled NER (TC-NER).
    REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
    REACT_1753. mRNA Splicing - Minor Pathway.
    REACT_1851. RNA Polymerase II Transcription Initiation.
    REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
    REACT_2089. RNA Polymerase II Promoter Escape.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_2222. Dual incision reaction in TC-NER.
    REACT_467. mRNA Splicing - Major Pathway.
    REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6233. Transcription of the HIV genome.
    REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
    REACT_6244. Pausing and recovery of HIV elongation.
    REACT_6253. RNA Polymerase II HIV Promoter Escape.
    REACT_6259. HIV elongation arrest and recovery.
    REACT_6261. Abortive elongation of HIV-1 transcript in the absence of Tat.
    REACT_6319. Formation of the HIV-1 Early Elongation Complex.
    REACT_6332. HIV Transcription Initiation.
    REACT_6344. Tat-mediated HIV elongation arrest and recovery.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_6354. Viral Messenger RNA Synthesis.
    REACT_833. RNA Polymerase II Transcription Elongation.
    REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
    REACT_846. Formation of the Early Elongation Complex.
    REACT_975. 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
    RNA-directed RNA polymerase II subunit RPB1 (EC:2.7.7.48)
    Gene namesi
    Name:POLR2A
    Synonyms:POLR2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:9187. POLR2A.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. DNA-directed RNA polymerase II, core complex Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    DNA-directed RNA polymerase, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1810 – 18101R → A: Misexpression of a variety of small nuclear RNAs and small nucleolar RNAs. 1 Publication

    Organism-specific databases

    MIMi180660. gene+phenotype.
    PharmGKBiPA33507.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 19701970DNA-directed RNA polymerase II subunit RPB1PRO_0000073940Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei1810 – 18101Omega-N-methylated arginine; by CARM11 Publication
    Modified residuei1843 – 18431Phosphoserine1 Publication
    Modified residuei1849 – 18491Phosphoserine1 Publication
    Modified residuei1854 – 18541Phosphothreonine1 Publication
    Modified residuei1874 – 18741Phosphotyrosine1 Publication
    Modified residuei1878 – 18781Phosphoserine1 Publication
    Modified residuei1882 – 18821Phosphoserine1 Publication
    Modified residuei1896 – 18961Phosphoserine1 Publication
    Modified residuei1899 – 18991Phosphoserine1 Publication
    Modified residuei1909 – 19091Phosphotyrosine2 Publications
    Modified residuei1913 – 19131Phosphoserine2 Publications
    Modified residuei1917 – 19171Phosphoserine2 Publications
    Modified residuei1920 – 19201Phosphoserine2 Publications
    Modified residuei1923 – 19231Phosphotyrosine2 Publications
    Modified residuei1927 – 19271Phosphoserine2 Publications
    Modified residuei1931 – 19311Phosphoserine2 Publications
    Modified residuei1933 – 19331PhosphothreonineBy similarity
    Modified residuei1934 – 19341Phosphoserine2 Publications

    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 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.
    Ubiquitinated by WWP2 leading to proteasomal degradation 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 similarity1 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.1 Publication

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP24928.
    PaxDbiP24928.
    PRIDEiP24928.

    PTM databases

    PhosphoSiteiP24928.

    Expressioni

    Gene expression databases

    ArrayExpressiP24928.
    BgeeiP24928.
    CleanExiHS_POLR2A.
    GenevestigatoriP24928.

    Organism-specific databases

    HPAiCAB012226.
    CAB016388.
    CAB022311.
    HPA021563.
    HPA053012.

    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 and MYO1C By similarity. Interacts with 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. Interacts with PAF1. Interacts (via C-terminus) with CMTR1, CTDSP1 and 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. Interacts with RECQL5 and TCEA1; binding of RECQL5 prevents TCEA1 binding. 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).By similarity21 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC73Q6P1J95EBI-295301,EBI-930143
    DDX5P178443EBI-295301,EBI-351962
    PAF1Q8N7H55EBI-295301,EBI-2607770
    RPRD1BQ9NQG55EBI-295301,EBI-747925
    SNF8Q96H202EBI-295301,EBI-747719
    SUPT5HO002672EBI-295301,EBI-710464
    XAB2Q9HCS72EBI-295301,EBI-295232

    Protein-protein interaction databases

    BioGridi111426. 216 interactions.
    DIPiDIP-29011N.
    IntActiP24928. 40 interactions.
    MINTiMINT-156582.
    STRINGi9606.ENSP00000314949.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GHQX-ray2.05C/D1795-1803[»]
    2GHTX-ray1.80C/D1796-1803[»]
    2LTONMR-B1804-1816[»]
    3D9KX-ray2.20Y/Z1790-1803[»]
    3D9LX-ray2.20Y/Z1790-1803[»]
    3D9MX-ray1.75Y/Z1790-1803[»]
    3D9NX-ray1.60Y/Z1790-1803[»]
    3D9OX-ray2.00Z1790-1803[»]
    3D9PX-ray2.10Y/Z1790-1803[»]
    4JXTX-ray1.90B1787-1805[»]
    ProteinModelPortaliP24928.
    SMRiP24928. Positions 16-896, 1072-1475.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24928.

    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-[SRTEVKGN]Add
    BLAST

    Sequence similaritiesi

    Belongs to the RNA polymerase beta' chain family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0086.
    HOGENOMiHOG000222975.
    HOVERGENiHBG004339.
    InParanoidiP24928.
    KOiK03006.
    OMAiIVFNRQP.
    OrthoDBiEOG7K0ZB8.
    PhylomeDBiP24928.
    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. 46 hits.
    [Graphical view]
    SMARTiSM00663. RPOLA_N. 1 hit.
    [Graphical view]
    PROSITEiPS00115. RNA_POL_II_REPEAT. 42 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P24928-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « 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 SYSPASPKYT PTSPSYSPSS 1850
    PEYTPTSPKY SPTSPKYSPT SPKYSPTSPT YSPTTPKYSP TSPTYSPTSP 1900
    VYTPTSPKYS PTSPTYSPTS PKYSPTSPTY SPTSPKGSTY SPTSPGYSPT 1950
    SPTYSLTSPA ISPDDSDEEN 1970
    Length:1,970
    Mass (Da):217,176
    Last modified:December 15, 2009 - v2
    Checksum:i28D6FD25693A6472
    GO
    Isoform 2 (identifier: P24928-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         558-566: GEVMNLLMF → VCGPNGNLA
         567-1970: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:566
    Mass (Da):63,641
    Checksum:i0F3049DAF63F3B20
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1067 – 10671W → L in CAA52862. (PubMed:7622068)Curated
    Sequence conflicti1449 – 14491D → Y in CAA52862. (PubMed:7622068)Curated
    Sequence conflicti1835 – 18351A → T in CAA45125. (PubMed:1542581)Curated
    Sequence conflicti1835 – 18351A → T in CAA52862. (PubMed:7622068)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti292 – 2921R → C.
    Corresponds to variant rs2229198 [ dbSNP | Ensembl ].
    VAR_051872

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei558 – 5669GEVMNLLMF → VCGPNGNLA in isoform 2. 1 PublicationVSP_056184
    Alternative sequencei567 – 19701404Missing in isoform 2. 1 PublicationVSP_056185Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63564 mRNA. Translation: CAA45125.1.
    X74874
    , X74873, X74872, X74871, X74870 Genomic DNA. Translation: CAA52862.1.
    AC113189 Genomic DNA. No translation available.
    CH471108 Genomic DNA. Translation: EAW90181.1.
    BC067295 mRNA. Translation: AAH67295.1.
    BC137231 mRNA. Translation: AAI37232.1.
    CCDSiCCDS32548.1.
    PIRiI38186.
    S21054.
    RefSeqiNP_000928.1. NM_000937.4.
    UniGeneiHs.270017.

    Genome annotation databases

    EnsembliENST00000322644; ENSP00000314949; ENSG00000181222.
    ENST00000572844; ENSP00000461879; ENSG00000181222.
    GeneIDi5430.
    KEGGihsa:5430.
    UCSCiuc002ghf.4. human.

    Polymorphism databases

    DMDMi281185484.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63564 mRNA. Translation: CAA45125.1 .
    X74874
    , X74873 , X74872 , X74871 , X74870 Genomic DNA. Translation: CAA52862.1 .
    AC113189 Genomic DNA. No translation available.
    CH471108 Genomic DNA. Translation: EAW90181.1 .
    BC067295 mRNA. Translation: AAH67295.1 .
    BC137231 mRNA. Translation: AAI37232.1 .
    CCDSi CCDS32548.1.
    PIRi I38186.
    S21054.
    RefSeqi NP_000928.1. NM_000937.4.
    UniGenei Hs.270017.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GHQ X-ray 2.05 C/D 1795-1803 [» ]
    2GHT X-ray 1.80 C/D 1796-1803 [» ]
    2LTO NMR - B 1804-1816 [» ]
    3D9K X-ray 2.20 Y/Z 1790-1803 [» ]
    3D9L X-ray 2.20 Y/Z 1790-1803 [» ]
    3D9M X-ray 1.75 Y/Z 1790-1803 [» ]
    3D9N X-ray 1.60 Y/Z 1790-1803 [» ]
    3D9O X-ray 2.00 Z 1790-1803 [» ]
    3D9P X-ray 2.10 Y/Z 1790-1803 [» ]
    4JXT X-ray 1.90 B 1787-1805 [» ]
    ProteinModelPortali P24928.
    SMRi P24928. Positions 16-896, 1072-1475.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111426. 216 interactions.
    DIPi DIP-29011N.
    IntActi P24928. 40 interactions.
    MINTi MINT-156582.
    STRINGi 9606.ENSP00000314949.

    Chemistry

    BindingDBi P24928.
    ChEMBLi CHEMBL1641353.

    PTM databases

    PhosphoSitei P24928.

    Polymorphism databases

    DMDMi 281185484.

    Proteomic databases

    MaxQBi P24928.
    PaxDbi P24928.
    PRIDEi P24928.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000322644 ; ENSP00000314949 ; ENSG00000181222 .
    ENST00000572844 ; ENSP00000461879 ; ENSG00000181222 .
    GeneIDi 5430.
    KEGGi hsa:5430.
    UCSCi uc002ghf.4. human.

    Organism-specific databases

    CTDi 5430.
    GeneCardsi GC17P007387.
    H-InvDB HIX0173727.
    HGNCi HGNC:9187. POLR2A.
    HPAi CAB012226.
    CAB016388.
    CAB022311.
    HPA021563.
    HPA053012.
    MIMi 180660. gene+phenotype.
    neXtProti NX_P24928.
    PharmGKBi PA33507.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0086.
    HOGENOMi HOG000222975.
    HOVERGENi HBG004339.
    InParanoidi P24928.
    KOi K03006.
    OMAi IVFNRQP.
    OrthoDBi EOG7K0ZB8.
    PhylomeDBi P24928.
    TreeFami TF103036.

    Enzyme and pathway databases

    Reactomei REACT_12417. MicroRNA (miRNA) biogenesis.
    REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
    REACT_1470. mRNA Capping.
    REACT_1628. Transcription-coupled NER (TC-NER).
    REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
    REACT_1753. mRNA Splicing - Minor Pathway.
    REACT_1851. RNA Polymerase II Transcription Initiation.
    REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
    REACT_2089. RNA Polymerase II Promoter Escape.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_2222. Dual incision reaction in TC-NER.
    REACT_467. mRNA Splicing - Major Pathway.
    REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6233. Transcription of the HIV genome.
    REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
    REACT_6244. Pausing and recovery of HIV elongation.
    REACT_6253. RNA Polymerase II HIV Promoter Escape.
    REACT_6259. HIV elongation arrest and recovery.
    REACT_6261. Abortive elongation of HIV-1 transcript in the absence of Tat.
    REACT_6319. Formation of the HIV-1 Early Elongation Complex.
    REACT_6332. HIV Transcription Initiation.
    REACT_6344. Tat-mediated HIV elongation arrest and recovery.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_6354. Viral Messenger RNA Synthesis.
    REACT_833. RNA Polymerase II Transcription Elongation.
    REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
    REACT_846. Formation of the Early Elongation Complex.
    REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

    Miscellaneous databases

    ChiTaRSi POLR2A. human.
    EvolutionaryTracei P24928.
    GeneWikii POLR2A.
    GenomeRNAii 5430.
    NextBioi 21009.
    PROi P24928.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P24928.
    Bgeei P24928.
    CleanExi HS_POLR2A.
    Genevestigatori P24928.

    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. 46 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. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "The human gene encoding the largest subunit of RNA polymerase II."
      Mita K., Tsuji H., Morimyo M., Takahashi E., Nenoi M., Ichimura S., Yamauchi M., Hongo E., Hayashi A.
      Gene 159:285-286(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Brain and Testis.
    6. "Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes."
      Kershnar E., Wu S.-Y., Chiang C.-M.
      J. Biol. Chem. 273:34444-34453(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE RNA POLYMERASE II CORE-COMPLEX, SUBCELLULAR LOCATION.
    7. Cited for: INTERACTION WITH SAFB.
    8. "A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription."
      Parada C.A., Roeder R.G.
      EMBO J. 18:3688-3701(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH HTATSF1; CCNT1; NCL; SUPT5H AND CDK9.
    9. "Tat-SF1 protein associates with RAP30 and human SPT5 proteins."
      Kim J.B., Yamaguchi Y., Wada T., Handa H., Sharp P.A.
      Mol. Cell. Biol. 19:5960-5968(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HTATSF1.
    10. "The structure of an FF domain from human HYPA/FBP11."
      Allen M., Friedler A., Schon O., Bycroft M.
      J. Mol. Biol. 323:411-416(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FNBP3.
    11. "Hyperphosphorylated C-terminal repeat domain-associating proteins in the nuclear proteome link transcription to DNA/chromatin modification and RNA processing."
      Carty S.M., Greenleaf A.L.
      Mol. Cell. Proteomics 1:598-610(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SYNCRIP.
    12. "Synergism between p68 RNA helicase and the transcriptional coactivators CBP and p300."
      Rossow K.L., Janknecht R.
      Oncogene 22:151-156(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDX5.
    13. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Cyclin L2, a novel RNA polymerase II-associated cyclin, is involved in pre-mRNA splicing and induces apoptosis of human hepatocellular carcinoma cells."
      Yang L., Li N., Wang C., Yu Y., Yuan L., Zhang M., Cao X.
      J. Biol. Chem. 279:11639-11648(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CCNL2.
    15. Cited for: INTERACTION WITH MEN1.
    16. "Expression of the C-terminal domain of novel human SR-A1 protein: interaction with the CTD domain of RNA polymerase II."
      Katsarou M.E., Papakyriakou A., Katsaros N., Scorilas A.
      Biochem. Biophys. Res. Commun. 334:61-68(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SFRS19.
    17. "Identification and characterization of a novel human histone H3 lysine 36 specific methyltransferase."
      Sun X.-J., Wei J., Wu X.-Y., Hu M., Wang L., Wang H.-H., Zhang Q.-H., Chen S.-J., Huang Q.-H., Chen Z.
      J. Biol. Chem. 280:35261-35271(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SETD2.
    18. "Solution structure of the Set2-Rpb1 interacting domain of human Set2 and its interaction with the hyperphosphorylated C-terminal domain of Rpb1."
      Li M., Phatnani H.P., Guan Z., Sage H., Greenleaf A.L., Zhou P.
      Proc. Natl. Acad. Sci. U.S.A. 102:17636-17641(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SETD2.
    19. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1909 AND TYR-1923, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "The human homologue of the RNA polymerase II-associated factor 1 (hPaf1), localized on the 19q13 amplicon, is associated with tumorigenesis."
      Moniaux N., Nemos C., Schmied B.M., Chauhan S.C., Deb S., Morikane K., Choudhury A., Vanlith M., Sutherlin M., Sikela J.M., Hollingsworth M.A., Batra S.K.
      Oncogene 25:3247-3257(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAF1 IN PAF1/RNA POLYMERASE II.
      Tissue: Fetal pancreas.
    21. "The Spt6 SH2 domain binds Ser2-P RNAPII to direct Iws1-dependent mRNA splicing and export."
      Yoh S.M., Cho H., Pickle L., Evans R.M., Jones K.A.
      Genes Dev. 21:160-174(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUPT6H, PHOSPHORYLATION.
    22. "The human interferon-regulated ISG95 protein interacts with RNA polymerase II and shows methyltransferase activity."
      Haline-Vaz T., Silva T.C.L., Zanchin N.I.T.
      Biochem. Biophys. Res. Commun. 372:719-724(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CMTR1.
    23. "Snapshots of the RNA processing factor SCAF8 bound to different phosphorylated forms of the carboxyl-terminal domain of RNA polymerase II."
      Becker R., Loll B., Meinhart A.
      J. Biol. Chem. 283:22659-22669(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SCAF8.
    24. "Transcription of hepatitis delta virus RNA by RNA polymerase II."
      Chang J., Nie X., Chang H.E., Han Z., Taylor J.
      J. Virol. 82:1118-1127(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS RNA-DIRECTED RNA POLYMERASE.
    25. "Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A Histone H3-Lys4 methyltransferase complex to transcription start sites of transcribed human genes."
      Lee J.H., Skalnik D.G.
      Mol. Cell. Biol. 28:609-618(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SETD1A; SETD1B AND WDR82.
    26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1849; TYR-1874; SER-1896; TYR-1909; SER-1913; SER-1920; TYR-1923; SER-1927 AND SER-1934, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated telomerase activity."
      Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S., Watanabe S., Saitoh N., Ito T., Nakao M.
      J. Biol. Chem. 284:5165-5174(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATF7IP.
    29. "TFIIH kinase places bivalent marks on the carboxy-terminal domain of RNA polymerase II."
      Akhtar M.S., Heidemann M., Tietjen J.R., Zhang D.W., Chapman R.D., Eick D., Ansari A.Z.
      Mol. Cell 34:387-393(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CDK7.
    30. "TFIIH-associated Cdk7 kinase functions in phosphorylation of C-terminal domain Ser7 residues, promoter-proximal pausing, and termination by RNA polymerase II."
      Glover-Cutter K., Larochelle S., Erickson B., Zhang C., Shokat K., Fisher R.P., Bentley D.L.
      Mol. Cell. Biol. 29:5455-5464(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CDK7 AND CDK9.
    31. "Binding to DNA of the RNA-polymerase II C-terminal domain allows discrimination between Cdk7 and Cdk9 phosphorylation."
      Lolli G.
      Nucleic Acids Res. 37:1260-1268(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CDK7.
    32. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1843; THR-1854; SER-1878; SER-1882; SER-1899; SER-1913; SER-1917; SER-1920; SER-1927; SER-1931 AND SER-1934, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    33. "RecQL5 promotes genome stabilization through two parallel mechanisms--interacting with RNA polymerase II and acting as a helicase."
      Islam M.N., Fox D. III, Guo R., Enomoto T., Wang W.
      Mol. Cell. Biol. 30:2460-2472(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RECQL5, FUNCTION.
    34. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    35. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    36. "Transcription factor IIS cooperates with the E3 ligase UBR5 to ubiquitinate the CDK9 subunit of the positive transcription elongation factor B."
      Cojocaru M., Bouchard A., Cloutier P., Cooper J.J., Varzavand K., Price D.H., Coulombe B.
      J. Biol. Chem. 286:5012-5022(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CDK9.
    37. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1917 AND SER-1931, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    38. "The C-terminal domain of RNA polymerase II is modified by site-specific methylation."
      Sims R.J. III, Rojas L.A., Beck D., Bonasio R., Schuller R., Drury W.J. III, Eick D., Reinberg D.
      Science 332:99-103(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT ARG-1810 BY CARM1, MUTAGENESIS OF ARG-1810.
    39. "Ser7 phosphorylation of the CTD recruits the RPAP2 Ser5 phosphatase to snRNA genes."
      Egloff S., Zaborowska J., Laitem C., Kiss T., Murphy S.
      Mol. Cell 45:111-122(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    40. "Mutations in UVSSA cause UV-sensitive syndrome and impair RNA polymerase IIo processing in transcription-coupled nucleotide-excision repair."
      Nakazawa Y., Sasaki K., Mitsutake N., Matsuse M., Shimada M., Nardo T., Takahashi Y., Ohyama K., Ito K., Mishima H., Nomura M., Kinoshita A., Ono S., Takenaka K., Masuyama R., Kudo T., Slor H., Utani A.
      , Tateishi S., Yamashita S., Stefanini M., Lehmann A.R., Yoshiura K.I., Ogi T.
      Nat. Genet. 44:586-592(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    41. "Determinants for dephosphorylation of the RNA polymerase II C-terminal domain by Scp1."
      Zhang Y., Kim Y., Genoud N., Gao J., Kelly J.W., Pfaff S.L., Gill G.N., Dixon J.E., Noel J.P.
      Mol. Cell 24:759-770(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1796-1803 IN COMPLEX WITH CTDSP1, DEPHOSPHORYLATION.
    42. "Structural mimicry in transcription regulation of human RNA polymerase II by the DNA helicase RECQL5."
      Kassube S.A., Jinek M., Fang J., Tsutakawa S., Nogales E.
      Nat. Struct. Mol. Biol. 20:892-899(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH RECQL5, INTERACTION WITH RECQL5 AND TCEA1, SUBUNIT, FUNCTION.

    Entry informationi

    Entry nameiRPB1_HUMAN
    AccessioniPrimary (citable) accession number: P24928
    Secondary accession number(s): A6NN93, B9EH88, Q6NX41
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: December 15, 2009
    Last modified: October 1, 2014
    This is version 161 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3