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P04050

- RPB1_YEAST

UniProt

P04050 - RPB1_YEAST

Protein

DNA-directed RNA polymerase II subunit RPB1

Gene

RPO21

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      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. During a transcription cycle, Pol II, general transcription factors and the Mediator complex assemble as the preinitiation complex (PIC) at the promoter. 11-15 base pairs of DNA surrounding the transcription start site are melted and the single-stranded DNA template strand of the promoter is positioned deeply within the central active site cleft of Pol II to form the open complex. After synthesis of about 30 bases of RNA, Pol II releases its contacts with the core promoter and the rest of the transcription machinery (promoter clearance) and enters the stage of transcription elongation in which it moves on the template as the transcript elongates. Pol II appears to oscillate between inactive and active conformations at each step of nucleotide addition. 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. Pol II is composed of mobile elements that move relative to each other. The core element with the central large cleft comprises RPB3, RBP10, RPB11, RPB12 and regions of RPB1 and RPB2 forming the active center. The clamp element (portions of RPB1, RPB2 and RPB3) is connected to the core through a set of flexible switches and moves to open and close the cleft. 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. In elongating Pol II, the lid loop (RPB1) appears to act as a wedge to drive apart the DNA and RNA strands at the upstream end of the transcription bubble and guide the RNA strand toward the RNA exit groove located near the base of the largely unstructured CTD domain of RPB1. The rudder loop (RPB1) interacts with single-stranded DNA after separation from the RNA strand, likely preventing reassociation with the exiting RNA. The cleft is surrounded by jaws: an upper jaw formed by portions of RBP1, RPB2 and RPB9, and a lower jaw, formed by RPB5 and portions of RBP1. The jaws are thought to grab the incoming DNA template, mainly by RPB5 direct contacts to DNA.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi67 – 671Zinc 1
    Metal bindingi70 – 701Zinc 1
    Metal bindingi77 – 771Zinc 1
    Metal bindingi80 – 801Zinc 1
    Metal bindingi107 – 1071Zinc 2
    Metal bindingi110 – 1101Zinc 2
    Metal bindingi148 – 1481Zinc 2
    Metal bindingi167 – 1671Zinc 2
    Metal bindingi481 – 4811Magnesium 1; catalytic
    Metal bindingi481 – 4811Magnesium 2; shared with RPB2
    Metal bindingi483 – 4831Magnesium 1; catalytic
    Metal bindingi483 – 4831Magnesium 2; shared with RPB2
    Metal bindingi485 – 4851Magnesium 1; catalytic

    GO - Molecular functioni

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

    GO - Biological processi

    1. transcription, RNA-templated Source: GOC
    2. transcription from RNA polymerase II promoter Source: SGD
    3. translesion synthesis Source: SGD

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Transcription

    Keywords - Ligandi

    DNA-binding, Magnesium, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29539-MONOMER.
    ReactomeiREACT_191540. mRNA Splicing - Minor Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA-directed RNA polymerase II subunit RPB1 (EC:2.7.7.6)
    Short name:
    RNA polymerase II subunit 1
    Short name:
    RNA polymerase II subunit B1
    Alternative name(s):
    DNA-directed RNA polymerase III largest subunit
    RNA polymerase II subunit B220
    Gene namesi
    Name:RPO21
    Synonyms:RPB1, RPB220, SUA8
    Ordered Locus Names:YDL140C
    ORF Names:D2150
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDL140c.
    SGDiS000002299. RPO21.

    Subcellular locationi

    GO - Cellular componenti

    1. DNA-directed RNA polymerase II, core complex Source: SGD

    Keywords - Cellular componenti

    DNA-directed RNA polymerase, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17331733DNA-directed RNA polymerase II subunit RPB1PRO_0000073946Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki695 – 695Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei1471 – 14711Phosphothreonine1 Publication

    Post-translational modificationi

    The tandem 7 residues repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat. The phosphorylated form of Pol II appears to carry, on average, one phosphate per repeat. The phosphorylation state is believed to result from the balanced action of site-specific CTD kinases and phosphataes, and a "CTD code" that specifies the position of Pol II within the transcription cycle has been proposed. Phosphorylation at 'Ser-5' occurs in promoter-proximal regions in early elongation. Phosphorylation at 'Ser-2' predominates in regions more distal to the promoter and triggers binding of the 3' RNA processing machinery. CTD kinases include KIN28 (as part of the TFKII complex, a subcomplex of the TFIIH holo complex), SSN3/SRB10 (as part of the SRB8-11 complex, a module of the Mediator complex), CTK1 (as part of CTD kinase), and probably BUR1 (as part of the BUR1-BUR2 kinase complex). Phosphatases include FCP1 and SSU72.4 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP04050.
    PaxDbiP04050.
    PeptideAtlasiP04050.

    Expressioni

    Gene expression databases

    GenevestigatoriP04050.

    Interactioni

    Subunit structurei

    Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits. Interacts with ASK10, ESS1, RTT103 and SHE2.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC73Q0669717EBI-15760,EBI-29913
    CTR9P891054EBI-15760,EBI-5283
    RTF1P530647EBI-15760,EBI-16303
    SEN1Q004163EBI-15760,EBI-16945
    SPT5P276923EBI-15760,EBI-17937

    Protein-protein interaction databases

    BioGridi31921. 298 interactions.
    DIPiDIP-611N.
    IntActiP04050. 40 interactions.
    MINTiMINT-432838.

    Structurei

    Secondary structure

    1
    1733
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 183
    Helixi24 – 296
    Beta strandi32 – 343
    Beta strandi39 – 413
    Beta strandi43 – 453
    Beta strandi46 – 483
    Beta strandi51 – 544
    Beta strandi56 – 583
    Beta strandi62 – 643
    Beta strandi67 – 693
    Turni74 – 763
    Beta strandi84 – 918
    Helixi93 – 953
    Helixi96 – 10510
    Turni108 – 1103
    Beta strandi113 – 1153
    Beta strandi117 – 1193
    Helixi120 – 1267
    Beta strandi127 – 1293
    Helixi131 – 14212
    Beta strandi150 – 1523
    Beta strandi160 – 1634
    Beta strandi173 – 1775
    Beta strandi181 – 1855
    Beta strandi187 – 1904
    Beta strandi198 – 2025
    Helixi204 – 2118
    Beta strandi212 – 2143
    Helixi216 – 2216
    Turni226 – 2283
    Helixi231 – 2344
    Beta strandi235 – 2395
    Turni244 – 2463
    Beta strandi253 – 2553
    Beta strandi257 – 2604
    Helixi261 – 28020
    Turni281 – 2833
    Helixi286 – 30419
    Beta strandi307 – 3104
    Beta strandi313 – 3164
    Beta strandi318 – 3214
    Helixi325 – 3295
    Turni330 – 3356
    Helixi338 – 3403
    Beta strandi341 – 3444
    Beta strandi347 – 3559
    Beta strandi363 – 3675
    Helixi368 – 3714
    Beta strandi375 – 3795
    Turni382 – 3843
    Helixi385 – 39410
    Turni395 – 3973
    Beta strandi398 – 4003
    Beta strandi402 – 4065
    Helixi408 – 4103
    Beta strandi412 – 4143
    Turni415 – 4173
    Turni419 – 4224
    Beta strandi431 – 4355
    Beta strandi441 – 4455
    Helixi452 – 4543
    Beta strandi455 – 47016
    Helixi472 – 4743
    Helixi475 – 4784
    Beta strandi482 – 4843
    Beta strandi486 – 4905
    Helixi495 – 50410
    Helixi507 – 5104
    Beta strandi511 – 5133
    Turni514 – 5174
    Beta strandi518 – 5203
    Helixi525 – 53511
    Beta strandi536 – 5383
    Beta strandi540 – 5423
    Helixi543 – 55210
    Beta strandi553 – 5553
    Beta strandi567 – 5693
    Beta strandi571 – 5733
    Helixi574 – 5818
    Beta strandi588 – 5903
    Beta strandi596 – 5983
    Beta strandi600 – 6023
    Beta strandi604 – 6085
    Beta strandi611 – 6155
    Helixi619 – 6224
    Beta strandi626 – 6283
    Helixi629 – 6379
    Helixi639 – 65820
    Helixi666 – 6694
    Helixi673 – 69927
    Beta strandi706 – 7083
    Helixi710 – 73627
    Helixi742 – 7498
    Beta strandi750 – 7523
    Helixi755 – 7628
    Beta strandi770 – 7745
    Beta strandi778 – 7814
    Beta strandi782 – 7843
    Turni794 – 7985
    Turni804 – 8063
    Helixi810 – 84536
    Beta strandi863 – 8675
    Helixi868 – 8703
    Helixi875 – 8773
    Beta strandi878 – 8825
    Helixi884 – 8863
    Helixi890 – 8978
    Beta strandi901 – 9033
    Turni904 – 9063
    Turni910 – 9123
    Beta strandi913 – 9153
    Helixi916 – 9194
    Helixi923 – 94624
    Turni947 – 9493
    Beta strandi953 – 9586
    Helixi960 – 97011
    Beta strandi975 – 9773
    Helixi983 – 99412
    Helixi1005 – 10139
    Helixi1016 – 102510
    Helixi1028 – 10336
    Helixi1039 – 105618
    Helixi1064 – 107613
    Beta strandi1079 – 10824
    Helixi1086 – 10883
    Beta strandi1089 – 10913
    Beta strandi1092 – 10943
    Helixi1097 – 11048
    Turni1105 – 11073
    Beta strandi1115 – 11206
    Beta strandi1122 – 11265
    Helixi1128 – 113811
    Helixi1143 – 11453
    Beta strandi1147 – 11548
    Beta strandi1158 – 11603
    Helixi1164 – 11663
    Helixi1167 – 11715
    Beta strandi1172 – 11743
    Beta strandi1179 – 11824
    Beta strandi1190 – 11978
    Helixi1199 – 12046
    Helixi1209 – 122012
    Helixi1221 – 12233
    Beta strandi1224 – 12285
    Beta strandi1233 – 12353
    Beta strandi1237 – 12426
    Helixi1258 – 127013
    Beta strandi1272 – 12754
    Beta strandi1282 – 129211
    Beta strandi1296 – 131015
    Helixi1313 – 13164
    Beta strandi1317 – 13226
    Turni1324 – 13263
    Beta strandi1328 – 13303
    Helixi1332 – 13398
    Helixi1341 – 135717
    Turni1358 – 13603
    Helixi1365 – 137410
    Turni1375 – 13773
    Beta strandi1378 – 13803
    Beta strandi1384 – 13863
    Beta strandi1388 – 13903
    Beta strandi1392 – 13943
    Helixi1396 – 13994
    Turni1400 – 14023
    Helixi1406 – 141510
    Helixi1424 – 14296
    Helixi1437 – 14393
    Beta strandi1440 – 14456
    Helixi1447 – 14504
    Beta strandi1677 – 16804

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1I3QX-ray3.10A1-1733[»]
    1I50X-ray2.80A1-1733[»]
    1I6HX-ray3.30A1-1733[»]
    1K83X-ray2.80A1-1733[»]
    1NIKX-ray4.10A1-1733[»]
    1NT9X-ray4.20A1-1733[»]
    1PQVX-ray3.80A1-1733[»]
    1R5UX-ray4.50A1-1733[»]
    1R9SX-ray4.25A1-1733[»]
    1R9TX-ray3.50A1-1733[»]
    1SFOX-ray3.61A1-1733[»]
    1TWAX-ray3.20A1-1733[»]
    1TWCX-ray3.00A1-1733[»]
    1TWFX-ray2.30A1-1733[»]
    1TWGX-ray3.30A1-1733[»]
    1TWHX-ray3.40A1-1733[»]
    1WCMX-ray3.80A1-1733[»]
    1Y1VX-ray3.80A1-1733[»]
    1Y1WX-ray4.00A1-1733[»]
    1Y1YX-ray4.00A1-1733[»]
    1Y77X-ray4.50A1-1733[»]
    2B63X-ray3.80A1-1733[»]
    2B8KX-ray4.15A1-1733[»]
    2E2HX-ray3.95A1-1733[»]
    2E2IX-ray3.41A1-1733[»]
    2E2JX-ray3.50A1-1733[»]
    2JA5X-ray3.80A1-1733[»]
    2JA6X-ray4.00A1-1733[»]
    2JA7X-ray3.80A/M1-1733[»]
    2JA8X-ray3.80A1-1733[»]
    2L0INMR-B1675-1688[»]
    2LO6NMR-B1675-1688[»]
    2NVQX-ray2.90A1-1733[»]
    2NVTX-ray3.36A1-1733[»]
    2NVXX-ray3.60A1-1733[»]
    2NVYX-ray3.40A1-1733[»]
    2NVZX-ray4.30A1-1733[»]
    2R7ZX-ray3.80A1-1733[»]
    2R92X-ray3.80A1-1733[»]
    2R93X-ray4.00A1-1733[»]
    2VUMX-ray3.40A1-1733[»]
    2YU9X-ray3.40A1-1733[»]
    3CQZX-ray2.80A1-1733[»]
    3FKIX-ray3.88A1-1733[»]
    3GTGX-ray3.78A1-1733[»]
    3GTJX-ray3.42A1-1733[»]
    3GTKX-ray3.80A1-1733[»]
    3GTLX-ray3.38A1-1733[»]
    3GTMX-ray3.80A1-1733[»]
    3GTOX-ray4.00A1-1733[»]
    3GTPX-ray3.90A1-1733[»]
    3GTQX-ray3.80A1-1733[»]
    3H3VX-ray4.00B1-1733[»]
    3HOUX-ray3.20A/M1-1733[»]
    3HOVX-ray3.50A1-1733[»]
    3HOWX-ray3.60A1-1733[»]
    3HOXX-ray3.65A1-1733[»]
    3HOYX-ray3.40A1-1733[»]
    3HOZX-ray3.65A1-1733[»]
    3I4MX-ray3.70A1-1733[»]
    3I4NX-ray3.90A1-1733[»]
    3J0Kelectron microscopy36.00A1-1455[»]
    3J1Nelectron microscopy16.00A1-1455[»]
    3K1FX-ray4.30A1-1733[»]
    3K7AX-ray3.80A1-1733[»]
    3M3YX-ray3.18A1-1733[»]
    3M4OX-ray3.57A1-1733[»]
    3PO2X-ray3.30A1-1733[»]
    3PO3X-ray3.30A1-1733[»]
    3QT1X-ray4.30A1-1733[»]
    3RZDX-ray3.30A1-1733[»]
    3RZOX-ray3.00A1-1733[»]
    3S14X-ray2.85A1-1733[»]
    3S15X-ray3.30A1-1733[»]
    3S16X-ray3.24A1-1733[»]
    3S17X-ray3.20A1-1733[»]
    3S1MX-ray3.13A1-1733[»]
    3S1NX-ray3.10A1-1733[»]
    3S1QX-ray3.30A1-1733[»]
    3S1RX-ray3.20A1-1733[»]
    3S2DX-ray3.20A1-1733[»]
    3S2HX-ray3.30A1-1733[»]
    4A3BX-ray3.50A1-1732[»]
    4A3CX-ray3.50A1-1732[»]
    4A3DX-ray3.40A1-1732[»]
    4A3EX-ray3.40A1-1732[»]
    4A3FX-ray3.50A1-1732[»]
    4A3GX-ray3.50A1-1732[»]
    4A3IX-ray3.80A1-1732[»]
    4A3JX-ray3.70A1-1732[»]
    4A3KX-ray3.50A1-1732[»]
    4A3LX-ray3.50A1-1732[»]
    4A3MX-ray3.90A1-1732[»]
    4A93X-ray3.40A1-1732[»]
    4BBRX-ray3.40A1-1733[»]
    4BBSX-ray3.60A1-1733[»]
    4BXXX-ray3.28A1-1733[»]
    4BXZX-ray4.80A1-1733[»]
    4BY1X-ray3.60A1-1733[»]
    4BY7X-ray3.15A1-1733[»]
    4GWQX-ray4.50H1619-1653[»]
    ProteinModelPortaliP04050.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04050.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati1549 – 155571
    Repeati1556 – 156272
    Repeati1563 – 156973
    Repeati1570 – 157674
    Repeati1577 – 158375
    Repeati1584 – 159076
    Repeati1591 – 159777
    Repeati1598 – 160478
    Repeati1605 – 161179
    Repeati1612 – 1618710
    Repeati1619 – 1625711
    Repeati1626 – 1632712
    Repeati1633 – 1639713
    Repeati1640 – 1646714
    Repeati1647 – 1653715
    Repeati1654 – 1660716
    Repeati1661 – 1667717
    Repeati1668 – 1674718
    Repeati1675 – 1681719
    Repeati1682 – 1688720
    Repeati1689 – 1695721
    Repeati1696 – 1702722
    Repeati1703 – 1709723
    Repeati1710 – 1716724; approximate

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni248 – 26013Lid loopAdd
    BLAST
    Regioni306 – 32318Rudder loopAdd
    BLAST
    Regioni810 – 82213Bridging helixAdd
    BLAST
    Regioni1549 – 171616824 X 7 AA approximate tandem repeats of Y-S-P-T-S-P-[A-S-N-G]Add
    BLAST

    Sequence similaritiesi

    Belongs to the RNA polymerase beta' chain family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0086.
    GeneTreeiENSGT00750000117852.
    HOGENOMiHOG000222975.
    KOiK03006.
    OMAiIVFNRQP.
    OrthoDBiEOG780RVQ.

    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. 16 hits.
    [Graphical view]
    SMARTiSM00663. RPOLA_N. 1 hit.
    [Graphical view]
    PROSITEiPS00115. RNA_POL_II_REPEAT. 22 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P04050-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVGQQYSSAP LRTVKEVQFG LFSPEEVRAI SVAKIRFPET MDETQTRAKI     50
    GGLNDPRLGS IDRNLKCQTC QEGMNECPGH FGHIDLAKPV FHVGFIAKIK 100
    KVCECVCMHC GKLLLDEHNE LMRQALAIKD SKKRFAAIWT LCKTKMVCET 150
    DVPSEDDPTQ LVSRGGCGNT QPTIRKDGLK LVGSWKKDRA TGDADEPELR 200
    VLSTEEILNI FKHISVKDFT SLGFNEVFSR PEWMILTCLP VPPPPVRPSI 250
    SFNESQRGED DLTFKLADIL KANISLETLE HNGAPHHAIE EAESLLQFHV 300
    ATYMDNDIAG QPQALQKSGR PVKSIRARLK GKEGRIRGNL MGKRVDFSAR 350
    TVISGDPNLE LDQVGVPKSI AKTLTYPEVV TPYNIDRLTQ LVRNGPNEHP 400
    GAKYVIRDSG DRIDLRYSKR AGDIQLQYGW KVERHIMDND PVLFNRQPSL 450
    HKMSMMAHRV KVIPYSTFRL NLSVTSPYNA DFDGDEMNLH VPQSEETRAE 500
    LSQLCAVPLQ IVSPQSNKPC MGIVQDTLCG IRKLTLRDTF IELDQVLNML 550
    YWVPDWDGVI PTPAIIKPKP LWSGKQILSV AIPNGIHLQR FDEGTTLLSP 600
    KDNGMLIIDG QIIFGVVEKK TVGSSNGGLI HVVTREKGPQ VCAKLFGNIQ 650
    KVVNFWLLHN GFSTGIGDTI ADGPTMREIT ETIAEAKKKV LDVTKEAQAN 700
    LLTAKHGMTL RESFEDNVVR FLNEARDKAG RLAEVNLKDL NNVKQMVMAG 750
    SKGSFINIAQ MSACVGQQSV EGKRIAFGFV DRTLPHFSKD DYSPESKGFV 800
    ENSYLRGLTP QEFFFHAMGG REGLIDTAVK TAETGYIQRR LVKALEDIMV 850
    HYDNTTRNSL GNVIQFIYGE DGMDAAHIEK QSLDTIGGSD AAFEKRYRVD 900
    LLNTDHTLDP SLLESGSEIL GDLKLQVLLD EEYKQLVKDR KFLREVFVDG 950
    EANWPLPVNI RRIIQNAQQT FHIDHTKPSD LTIKDIVLGV KDLQENLLVL 1000
    RGKNEIIQNA QRDAVTLFCC LLRSRLATRR VLQEYRLTKQ AFDWVLSNIE 1050
    AQFLRSVVHP GEMVGVLAAQ SIGEPATQMT LNTFHFAGVA SKKVTSGVPR 1100
    LKEILNVAKN MKTPSLTVYL EPGHAADQEQ AKLIRSAIEH TTLKSVTIAS 1150
    EIYYDPDPRS TVIPEDEEII QLHFSLLDEE AEQSFDQQSP WLLRLELDRA 1200
    AMNDKDLTMG QVGERIKQTF KNDLFVIWSE DNDEKLIIRC RVVRPKSLDA 1250
    ETEAEEDHML KKIENTMLEN ITLRGVENIE RVVMMKYDRK VPSPTGEYVK 1300
    EPEWVLETDG VNLSEVMTVP GIDPTRIYTN SFIDIMEVLG IEAGRAALYK 1350
    EVYNVIASDG SYVNYRHMAL LVDVMTTQGG LTSVTRHGFN RSNTGALMRC 1400
    SFEETVEILF EAGASAELDD CRGVSENVIL GQMAPIGTGA FDVMIDEESL 1450
    VKYMPEQKIT EIEDGQDGGV TPYSNESGLV NADLDVKDEL MFSPLVDSGS 1500
    NDAMAGGFTA YGGADYGEAT SPFGAYGEAP TSPGFGVSSP GFSPTSPTYS 1550
    PTSPAYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP 1600
    TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT 1650
    SPSYSPTSPA YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS PTSPNYSPTS 1700
    PSYSPTSPGY SPGSPAYSPK QDEQKHNENE NSR 1733
    Length:1,733
    Mass (Da):191,612
    Last modified:November 1, 1997 - v2
    Checksum:iA45C1360FF99F968
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1514 – 15141A → V in CAA26904. (PubMed:3896517)Curated
    Sequence conflicti1524 – 15241G → A in CAA26904. (PubMed:3896517)Curated
    Sequence conflicti1601 – 16011T → M(PubMed:3896517)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1653 – 16597Missing in strain: A364A.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03128 Genomic DNA. Translation: CAA26904.1.
    X96876 Genomic DNA. Translation: CAA65619.1.
    Z74188 Genomic DNA. Translation: CAA98713.1.
    U27182 Genomic DNA. Translation: AAC49058.1.
    BK006938 Genomic DNA. Translation: DAA11718.1.
    PIRiS67686. RNBY2L.
    RefSeqiNP_010141.1. NM_001180200.1.

    Genome annotation databases

    EnsemblFungiiYDL140C; YDL140C; YDL140C.
    GeneIDi851415.
    KEGGisce:YDL140C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03128 Genomic DNA. Translation: CAA26904.1 .
    X96876 Genomic DNA. Translation: CAA65619.1 .
    Z74188 Genomic DNA. Translation: CAA98713.1 .
    U27182 Genomic DNA. Translation: AAC49058.1 .
    BK006938 Genomic DNA. Translation: DAA11718.1 .
    PIRi S67686. RNBY2L.
    RefSeqi NP_010141.1. NM_001180200.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1I3Q X-ray 3.10 A 1-1733 [» ]
    1I50 X-ray 2.80 A 1-1733 [» ]
    1I6H X-ray 3.30 A 1-1733 [» ]
    1K83 X-ray 2.80 A 1-1733 [» ]
    1NIK X-ray 4.10 A 1-1733 [» ]
    1NT9 X-ray 4.20 A 1-1733 [» ]
    1PQV X-ray 3.80 A 1-1733 [» ]
    1R5U X-ray 4.50 A 1-1733 [» ]
    1R9S X-ray 4.25 A 1-1733 [» ]
    1R9T X-ray 3.50 A 1-1733 [» ]
    1SFO X-ray 3.61 A 1-1733 [» ]
    1TWA X-ray 3.20 A 1-1733 [» ]
    1TWC X-ray 3.00 A 1-1733 [» ]
    1TWF X-ray 2.30 A 1-1733 [» ]
    1TWG X-ray 3.30 A 1-1733 [» ]
    1TWH X-ray 3.40 A 1-1733 [» ]
    1WCM X-ray 3.80 A 1-1733 [» ]
    1Y1V X-ray 3.80 A 1-1733 [» ]
    1Y1W X-ray 4.00 A 1-1733 [» ]
    1Y1Y X-ray 4.00 A 1-1733 [» ]
    1Y77 X-ray 4.50 A 1-1733 [» ]
    2B63 X-ray 3.80 A 1-1733 [» ]
    2B8K X-ray 4.15 A 1-1733 [» ]
    2E2H X-ray 3.95 A 1-1733 [» ]
    2E2I X-ray 3.41 A 1-1733 [» ]
    2E2J X-ray 3.50 A 1-1733 [» ]
    2JA5 X-ray 3.80 A 1-1733 [» ]
    2JA6 X-ray 4.00 A 1-1733 [» ]
    2JA7 X-ray 3.80 A/M 1-1733 [» ]
    2JA8 X-ray 3.80 A 1-1733 [» ]
    2L0I NMR - B 1675-1688 [» ]
    2LO6 NMR - B 1675-1688 [» ]
    2NVQ X-ray 2.90 A 1-1733 [» ]
    2NVT X-ray 3.36 A 1-1733 [» ]
    2NVX X-ray 3.60 A 1-1733 [» ]
    2NVY X-ray 3.40 A 1-1733 [» ]
    2NVZ X-ray 4.30 A 1-1733 [» ]
    2R7Z X-ray 3.80 A 1-1733 [» ]
    2R92 X-ray 3.80 A 1-1733 [» ]
    2R93 X-ray 4.00 A 1-1733 [» ]
    2VUM X-ray 3.40 A 1-1733 [» ]
    2YU9 X-ray 3.40 A 1-1733 [» ]
    3CQZ X-ray 2.80 A 1-1733 [» ]
    3FKI X-ray 3.88 A 1-1733 [» ]
    3GTG X-ray 3.78 A 1-1733 [» ]
    3GTJ X-ray 3.42 A 1-1733 [» ]
    3GTK X-ray 3.80 A 1-1733 [» ]
    3GTL X-ray 3.38 A 1-1733 [» ]
    3GTM X-ray 3.80 A 1-1733 [» ]
    3GTO X-ray 4.00 A 1-1733 [» ]
    3GTP X-ray 3.90 A 1-1733 [» ]
    3GTQ X-ray 3.80 A 1-1733 [» ]
    3H3V X-ray 4.00 B 1-1733 [» ]
    3HOU X-ray 3.20 A/M 1-1733 [» ]
    3HOV X-ray 3.50 A 1-1733 [» ]
    3HOW X-ray 3.60 A 1-1733 [» ]
    3HOX X-ray 3.65 A 1-1733 [» ]
    3HOY X-ray 3.40 A 1-1733 [» ]
    3HOZ X-ray 3.65 A 1-1733 [» ]
    3I4M X-ray 3.70 A 1-1733 [» ]
    3I4N X-ray 3.90 A 1-1733 [» ]
    3J0K electron microscopy 36.00 A 1-1455 [» ]
    3J1N electron microscopy 16.00 A 1-1455 [» ]
    3K1F X-ray 4.30 A 1-1733 [» ]
    3K7A X-ray 3.80 A 1-1733 [» ]
    3M3Y X-ray 3.18 A 1-1733 [» ]
    3M4O X-ray 3.57 A 1-1733 [» ]
    3PO2 X-ray 3.30 A 1-1733 [» ]
    3PO3 X-ray 3.30 A 1-1733 [» ]
    3QT1 X-ray 4.30 A 1-1733 [» ]
    3RZD X-ray 3.30 A 1-1733 [» ]
    3RZO X-ray 3.00 A 1-1733 [» ]
    3S14 X-ray 2.85 A 1-1733 [» ]
    3S15 X-ray 3.30 A 1-1733 [» ]
    3S16 X-ray 3.24 A 1-1733 [» ]
    3S17 X-ray 3.20 A 1-1733 [» ]
    3S1M X-ray 3.13 A 1-1733 [» ]
    3S1N X-ray 3.10 A 1-1733 [» ]
    3S1Q X-ray 3.30 A 1-1733 [» ]
    3S1R X-ray 3.20 A 1-1733 [» ]
    3S2D X-ray 3.20 A 1-1733 [» ]
    3S2H X-ray 3.30 A 1-1733 [» ]
    4A3B X-ray 3.50 A 1-1732 [» ]
    4A3C X-ray 3.50 A 1-1732 [» ]
    4A3D X-ray 3.40 A 1-1732 [» ]
    4A3E X-ray 3.40 A 1-1732 [» ]
    4A3F X-ray 3.50 A 1-1732 [» ]
    4A3G X-ray 3.50 A 1-1732 [» ]
    4A3I X-ray 3.80 A 1-1732 [» ]
    4A3J X-ray 3.70 A 1-1732 [» ]
    4A3K X-ray 3.50 A 1-1732 [» ]
    4A3L X-ray 3.50 A 1-1732 [» ]
    4A3M X-ray 3.90 A 1-1732 [» ]
    4A93 X-ray 3.40 A 1-1732 [» ]
    4BBR X-ray 3.40 A 1-1733 [» ]
    4BBS X-ray 3.60 A 1-1733 [» ]
    4BXX X-ray 3.28 A 1-1733 [» ]
    4BXZ X-ray 4.80 A 1-1733 [» ]
    4BY1 X-ray 3.60 A 1-1733 [» ]
    4BY7 X-ray 3.15 A 1-1733 [» ]
    4GWQ X-ray 4.50 H 1619-1653 [» ]
    ProteinModelPortali P04050.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31921. 298 interactions.
    DIPi DIP-611N.
    IntActi P04050. 40 interactions.
    MINTi MINT-432838.

    Proteomic databases

    MaxQBi P04050.
    PaxDbi P04050.
    PeptideAtlasi P04050.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDL140C ; YDL140C ; YDL140C .
    GeneIDi 851415.
    KEGGi sce:YDL140C.

    Organism-specific databases

    CYGDi YDL140c.
    SGDi S000002299. RPO21.

    Phylogenomic databases

    eggNOGi COG0086.
    GeneTreei ENSGT00750000117852.
    HOGENOMi HOG000222975.
    KOi K03006.
    OMAi IVFNRQP.
    OrthoDBi EOG780RVQ.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29539-MONOMER.
    Reactomei REACT_191540. mRNA Splicing - Minor Pathway.

    Miscellaneous databases

    EvolutionaryTracei P04050.
    NextBioi 968606.
    PROi P04050.

    Gene expression databases

    Genevestigatori P04050.

    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. 16 hits.
    [Graphical view ]
    SMARTi SM00663. RPOLA_N. 1 hit.
    [Graphical view ]
    PROSITEi PS00115. RNA_POL_II_REPEAT. 22 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Extensive homology among the largest subunits of eukaryotic and prokaryotic RNA polymerases."
      Allison L.A., Moyle M., Shales M., Ingles C.J.
      Cell 42:599-610(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204626 / S288c / A364A.
    2. "Analysis of a 26,756 bp segment from the left arm of yeast chromosome IV."
      Woelfl S., Haneman V., Saluz H.P.
      Yeast 12:1549-1554(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "The gene encoding the biotin-apoprotein ligase of Saccharomyces cerevisiae."
      Cronan J.E. Jr., Wallace J.C.
      FEMS Microbiol. Lett. 130:221-230(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1669-1733.
      Strain: ATCC 204508 / S288c.
    6. "Construction and analysis of yeast RNA polymerase II CTD deletion and substitution mutations."
      West M.L., Corden J.L.
      Genetics 140:1223-1233(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF THE CTD.
    7. "Temporal regulation of RNA polymerase II by Srb10 and Kin28 cyclin-dependent kinases."
      Hengartner C.J., Myer V.E., Liao S.-M., Wilson C.J., Koh S.S., Young R.A.
      Mol. Cell 2:43-53(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY THE TFIIK COMPLEX AND THE SRB8-11 COMPLEX.
    8. "Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3'-End formation."
      Morris D.P., Phatnani H.P., Greenleaf A.L.
      J. Biol. Chem. 274:31583-31587(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ESS1.
    9. "An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae."
      Kobor M.S., Archambault J., Lester W., Holstege F.C.P., Gileadi O., Jansma D.B., Jennings E.G., Kouyoumdjian F., Davidson A.R., Young R.A., Greenblatt J.
      Mol. Cell 4:55-62(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEPHOSPHORYLATION BY FCP1.
    10. "Phosphorylation of the RNA polymerase II carboxy-terminal domain by the Bur1 cyclin-dependent kinase."
      Murray S., Udupa R., Yao S., Hartzog G., Prelich G.
      Mol. Cell. Biol. 21:4089-4096(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY THE BUR KINASE COMPLEX.
    11. "Ask10p mediates the oxidative stress-induced destruction of the Saccharomyces cerevisiae C-type cyclin Ume3p/Srb11p."
      Cohen T.J., Lee K., Rutkowski L.H., Strich R.
      Eukaryot. Cell 2:962-970(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ASK10.
    12. "A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
      Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
      Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-695.
    13. "C-terminal repeat domain kinase I phosphorylates Ser2 and Ser5 of RNA polymerase II C-terminal domain repeats."
      Jones J.C., Phatnani H.P., Haystead T.A., MacDonald J.A., Alam S.M., Greenleaf A.L.
      J. Biol. Chem. 279:24957-24964(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CTD KINASE.
    14. "The yeast Rat1 exonuclease promotes transcription termination by RNA polymerase II."
      Kim M., Krogan N.J., Vasiljeva L., Rando O.J., Nedea E., Greenblatt J.F., Buratowski S.
      Nature 432:517-522(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RTT103.
    15. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    16. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1471, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Cotranscriptional recruitment of She2p by RNA pol II elongation factor Spt4-Spt5/DSIF promotes mRNA localization to the yeast bud."
      Shen Z., St-Denis A., Chartrand P.
      Genes Dev. 24:1914-1926(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHE2.
    18. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "RNA polymerase II/TFIIF structure and conserved organization of the initiation complex."
      Chung W.H., Craighead J.L., Chang W.H., Ezeokonkwo C., Bareket-Samish A., Kornberg R.D., Asturias F.J.
      Mol. Cell 12:1003-1013(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ELECTRON MICROSCOPY OF THE RNA POL II/TFIIF COMPLEX.
    20. "Structural basis of transcription: RNA polymerase II at 2.8 A resolution."
      Cramer P., Bushnell D.A., Kornberg R.D.
      Science 292:1863-1876(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
    21. "Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution."
      Gnatt A.L., Cramer P., Fu J., Bushnell D.A., Kornberg R.D.
      Science 292:1876-1882(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
    22. "Structural basis of transcription: alpha-amanitin-RNA polymerase II cocrystal at 2.8 A resolution."
      Bushnell D.A., Cramer P., Kornberg R.D.
      Proc. Natl. Acad. Sci. U.S.A. 99:1218-1222(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE RNA POL II CORE COMPLEX IN COMPLEX WITH ALPHA-AMANITIN.
    23. "Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage."
      Kettenberger H., Armache K.J., Cramer P.
      Cell 114:347-357(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX IN COMPLEX WITH DST1.
    24. "Architecture of initiation-competent 12-subunit RNA polymerase II."
      Armache K.J., Kettenberger H., Cramer P.
      Proc. Natl. Acad. Sci. U.S.A. 100:6964-6968(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS) OF THE RNA POL II COMPLEX.
    25. "Complete, 12-subunit RNA polymerase II at 4.1-A resolution: implications for the initiation of transcription."
      Bushnell D.A., Kornberg R.D.
      Proc. Natl. Acad. Sci. U.S.A. 100:6969-6973(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
    26. "Structural basis of transcription: nucleotide selection by rotation in the RNA polymerase II active center."
      Westover K.D., Bushnell D.A., Kornberg R.D.
      Cell 119:481-489(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
    27. "Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS."
      Kettenberger H., Armache K.J., Cramer P.
      Mol. Cell 16:955-965(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS).
    28. "Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 Angstroms."
      Bushnell D.A., Westover K.D., Davis R.E., Kornberg R.D.
      Science 303:983-988(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
    29. "Structures of complete RNA polymerase II and its subcomplex, Rpb4/7."
      Armache K.J., Mitterweger S., Meinhart A., Cramer P.
      J. Biol. Chem. 280:7131-7134(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX.
    30. "Structure of an RNA polymerase II-RNA inhibitor complex elucidates transcription regulation by noncoding RNAs."
      Kettenberger H., Eisenfuhr A., Brueckner F., Theis M., Famulok M., Cramer P.
      Nat. Struct. Mol. Biol. 13:44-48(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX IN COMPLEX WITH INHIBITING NON-CODING RNA.
    31. "Phasing RNA polymerase II using intrinsically bound Zn atoms: an updated structural model."
      Meyer P.A., Ye P., Zhang M., Suh M.H., Fu J.
      Structure 14:973-982(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (4.15 ANGSTROMS) OF THE RNA POL II COMPLEX.

    Entry informationi

    Entry nameiRPB1_YEAST
    AccessioniPrimary (citable) accession number: P04050
    Secondary accession number(s): D6VRK8, Q12364, Q92315
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1986
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 168 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Mutagenesis experiments demonstrate that the minimum viable CTD contains eight consensus Y-S-P-T-S-P-[A-S-N-G] heptapeptide repeats. Identical and simultaneous substitutions in a number of consecutive repeats are lethal: 'Ser-2' -> 'Ala-2' (14 repeats), 'Ser-5' -> 'Ala-5' (15 repeats), '2-Ser-Pro-Thr-Ser-5'-> '2-Ala-Pro-Thr-Ala-5' (10 repeats), 'Ser-2'-> 'Glu-2' (15 repeats), 'Ser-5' -> 'Glu-5' (12 repeats), '2-Ser-Pro-3' -> '2-Pro-Ser-3' (15 repeats) and 'Tyr-1' -> 'Phe-1' (12 repeats).
    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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3