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RPB11_YEAST
ID   RPB11_YEAST             Reviewed;         120 AA.
AC   P38902; D6W262;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 198.
DE   RecName: Full=DNA-directed RNA polymerase II subunit RPB11;
DE            Short=RNA polymerase II subunit B11;
DE   AltName: Full=B13.6;
DE   AltName: Full=DNA-directed RNA polymerase II 13.6 kDa polypeptide;
GN   Name=RPB11; OrderedLocusNames=YOL005C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 27-37; 75-84;
RP   98-102 AND 103-116.
RC   STRAIN=X2180-2;
RX   PubMed=8508029;
RA   Woychik N.A., McKune K., Lane W.S., Young R.A.;
RT   "Yeast RNA polymerase II subunit RPB11 is related to a subunit shared by
RT   RNA polymerase I and III.";
RL   Gene Expr. 3:77-82(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   FUNCTION, AND MUTAGENESIS OF GLU-108; LEU-111 AND LEU-114.
RX   PubMed=16537912; DOI=10.1128/mcb.26.7.2688-2696.2006;
RA   Steinmetz E.J., Ng S.B., Cloute J.P., Brow D.A.;
RT   "cis- and trans-Acting determinants of transcription termination by yeast
RT   RNA polymerase II.";
RL   Mol. Cell. Biol. 26:2688-2696(2006).
RN   [7]
RP   ELECTRON MICROSCOPY OF THE RNA POL II/TFIIF COMPLEX.
RX   PubMed=14580350; DOI=10.1016/s1097-2765(03)00387-3;
RA   Chung W.H., Craighead J.L., Chang W.H., Ezeokonkwo C., Bareket-Samish A.,
RA   Kornberg R.D., Asturias F.J.;
RT   "RNA polymerase II/TFIIF structure and conserved organization of the
RT   initiation complex.";
RL   Mol. Cell 12:1003-1013(2003).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
RX   PubMed=11313498; DOI=10.1126/science.1059493;
RA   Cramer P., Bushnell D.A., Kornberg R.D.;
RT   "Structural basis of transcription: RNA polymerase II at 2.8 A
RT   resolution.";
RL   Science 292:1863-1876(2001).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
RX   PubMed=11313499; DOI=10.1126/science.1059495;
RA   Gnatt A.L., Cramer P., Fu J., Bushnell D.A., Kornberg R.D.;
RT   "Structural basis of transcription: an RNA polymerase II elongation complex
RT   at 3.3 A resolution.";
RL   Science 292:1876-1882(2001).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE RNA POL II CORE COMPLEX IN
RP   COMPLEX WITH ALPHA-AMANITIN.
RX   PubMed=11805306; DOI=10.1073/pnas.251664698;
RA   Bushnell D.A., Cramer P., Kornberg R.D.;
RT   "Structural basis of transcription: alpha-amanitin-RNA polymerase II
RT   cocrystal at 2.8 A resolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:1218-1222(2002).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX IN COMPLEX
RP   WITH DST1.
RX   PubMed=12914699; DOI=10.1016/s0092-8674(03)00598-1;
RA   Kettenberger H., Armache K.J., Cramer P.;
RT   "Architecture of the RNA polymerase II-TFIIS complex and implications for
RT   mRNA cleavage.";
RL   Cell 114:347-357(2003).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS) OF THE RNA POL II COMPLEX.
RX   PubMed=12746495; DOI=10.1073/pnas.1030608100;
RA   Armache K.J., Kettenberger H., Cramer P.;
RT   "Architecture of initiation-competent 12-subunit RNA polymerase II.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:6964-6968(2003).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
RX   PubMed=12746498; DOI=10.1073/pnas.1130601100;
RA   Bushnell D.A., Kornberg R.D.;
RT   "Complete, 12-subunit RNA polymerase II at 4.1-A resolution: implications
RT   for the initiation of transcription.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:6969-6973(2003).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
RX   PubMed=15537538; DOI=10.1016/j.cell.2004.10.016;
RA   Westover K.D., Bushnell D.A., Kornberg R.D.;
RT   "Structural basis of transcription: nucleotide selection by rotation in the
RT   RNA polymerase II active center.";
RL   Cell 119:481-489(2004).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS).
RX   PubMed=15610738; DOI=10.1016/j.molcel.2004.11.040;
RA   Kettenberger H., Armache K.J., Cramer P.;
RT   "Complete RNA polymerase II elongation complex structure and its
RT   interactions with NTP and TFIIS.";
RL   Mol. Cell 16:955-965(2004).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
RX   PubMed=14963322; DOI=10.1126/science.1090838;
RA   Bushnell D.A., Westover K.D., Davis R.E., Kornberg R.D.;
RT   "Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at
RT   4.5 Angstroms.";
RL   Science 303:983-988(2004).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX.
RX   PubMed=15591044; DOI=10.1074/jbc.m413038200;
RA   Armache K.J., Mitterweger S., Meinhart A., Cramer P.;
RT   "Structures of complete RNA polymerase II and its subcomplex, Rpb4/7.";
RL   J. Biol. Chem. 280:7131-7134(2005).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX IN COMPLEX
RP   WITH INHIBITING NON-CODING RNA.
RX   PubMed=16341226; DOI=10.1038/nsmb1032;
RA   Kettenberger H., Eisenfuhr A., Brueckner F., Theis M., Famulok M.,
RA   Cramer P.;
RT   "Structure of an RNA polymerase II-RNA inhibitor complex elucidates
RT   transcription regulation by noncoding RNAs.";
RL   Nat. Struct. Mol. Biol. 13:44-48(2006).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (4.15 ANGSTROMS) OF THE RNA POL II COMPLEX.
RX   PubMed=16765890; DOI=10.1016/j.str.2006.04.003;
RA   Meyer P.A., Ye P., Zhang M., Suh M.H., Fu J.;
RT   "Phasing RNA polymerase II using intrinsically bound Zn atoms: an updated
RT   structural model.";
RL   Structure 14:973-982(2006).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       Component of RNA polymerase II which synthesizes mRNA precursors and
CC       many functional non-coding RNAs. Pol II is the central component of the
CC       basal RNA polymerase II transcription machinery. It is composed of
CC       mobile elements that move relative to each other. RPB11 is part of the
CC       core element with the central large cleft. Seems to be involved
CC       transcript termination. {ECO:0000269|PubMed:16537912}.
CC   -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC       of 12 subunits. {ECO:0000269|PubMed:11805306,
CC       ECO:0000269|PubMed:12914699, ECO:0000269|PubMed:16341226}.
CC   -!- INTERACTION:
CC       P38902; P16370: RPB3; NbExp=4; IntAct=EBI-15806, EBI-15773;
CC       P38902; P20436: RPB8; NbExp=3; IntAct=EBI-15806, EBI-15794;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 4280 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA
CC       polymerase subunit family. {ECO:0000305}.
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DR   EMBL; S62624; AAB27135.1; -; Genomic_DNA.
DR   EMBL; Z74747; CAA99004.1; -; Genomic_DNA.
DR   EMBL; AY557998; AAS56324.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10778.1; -; Genomic_DNA.
DR   PIR; S58933; S58933.
DR   RefSeq; NP_014638.1; NM_001183259.1.
DR   PDB; 1I3Q; X-ray; 3.10 A; K=1-120.
DR   PDB; 1I50; X-ray; 2.80 A; K=1-120.
DR   PDB; 1I6H; X-ray; 3.30 A; K=1-120.
DR   PDB; 1K83; X-ray; 2.80 A; K=1-120.
DR   PDB; 1NIK; X-ray; 4.10 A; K=1-120.
DR   PDB; 1NT9; X-ray; 4.20 A; K=1-120.
DR   PDB; 1PQV; X-ray; 3.80 A; K=1-120.
DR   PDB; 1R5U; X-ray; 4.50 A; K=1-120.
DR   PDB; 1R9S; X-ray; 4.25 A; K=1-120.
DR   PDB; 1R9T; X-ray; 3.50 A; K=1-120.
DR   PDB; 1SFO; X-ray; 3.61 A; K=1-120.
DR   PDB; 1TWA; X-ray; 3.20 A; K=1-120.
DR   PDB; 1TWC; X-ray; 3.00 A; K=1-120.
DR   PDB; 1TWF; X-ray; 2.30 A; K=1-120.
DR   PDB; 1TWG; X-ray; 3.30 A; K=1-120.
DR   PDB; 1TWH; X-ray; 3.40 A; K=1-120.
DR   PDB; 1WCM; X-ray; 3.80 A; K=1-120.
DR   PDB; 1Y1V; X-ray; 3.80 A; K=1-120.
DR   PDB; 1Y1W; X-ray; 4.00 A; K=1-120.
DR   PDB; 1Y1Y; X-ray; 4.00 A; K=1-120.
DR   PDB; 1Y77; X-ray; 4.50 A; K=1-120.
DR   PDB; 2B63; X-ray; 3.80 A; K=1-120.
DR   PDB; 2B8K; X-ray; 4.15 A; K=1-120.
DR   PDB; 2E2H; X-ray; 3.95 A; K=1-120.
DR   PDB; 2E2I; X-ray; 3.41 A; K=1-120.
DR   PDB; 2E2J; X-ray; 3.50 A; K=1-120.
DR   PDB; 2JA5; X-ray; 3.80 A; K=1-120.
DR   PDB; 2JA6; X-ray; 4.00 A; K=1-120.
DR   PDB; 2JA7; X-ray; 3.80 A; K/W=1-120.
DR   PDB; 2JA8; X-ray; 3.80 A; K=1-120.
DR   PDB; 2NVQ; X-ray; 2.90 A; K=1-120.
DR   PDB; 2NVT; X-ray; 3.36 A; K=1-120.
DR   PDB; 2NVX; X-ray; 3.60 A; K=1-120.
DR   PDB; 2NVY; X-ray; 3.40 A; K=1-120.
DR   PDB; 2NVZ; X-ray; 4.30 A; K=1-120.
DR   PDB; 2R7Z; X-ray; 3.80 A; K=1-120.
DR   PDB; 2R92; X-ray; 3.80 A; K=1-120.
DR   PDB; 2R93; X-ray; 4.00 A; K=1-120.
DR   PDB; 2VUM; X-ray; 3.40 A; K=1-120.
DR   PDB; 2YU9; X-ray; 3.40 A; K=1-120.
DR   PDB; 3CQZ; X-ray; 2.80 A; K=1-120.
DR   PDB; 3FKI; X-ray; 3.88 A; K=1-120.
DR   PDB; 3GTG; X-ray; 3.78 A; K=1-120.
DR   PDB; 3GTJ; X-ray; 3.42 A; K=1-120.
DR   PDB; 3GTK; X-ray; 3.80 A; K=1-120.
DR   PDB; 3GTL; X-ray; 3.38 A; K=1-120.
DR   PDB; 3GTM; X-ray; 3.80 A; K=1-120.
DR   PDB; 3GTO; X-ray; 4.00 A; K=1-120.
DR   PDB; 3GTP; X-ray; 3.90 A; K=1-120.
DR   PDB; 3GTQ; X-ray; 3.80 A; K=1-120.
DR   PDB; 3H3V; X-ray; 4.00 A; L=1-120.
DR   PDB; 3HOU; X-ray; 3.20 A; K/W=1-120.
DR   PDB; 3HOV; X-ray; 3.50 A; K=1-120.
DR   PDB; 3HOW; X-ray; 3.60 A; K=1-120.
DR   PDB; 3HOX; X-ray; 3.65 A; K=1-120.
DR   PDB; 3HOY; X-ray; 3.40 A; K=1-120.
DR   PDB; 3HOZ; X-ray; 3.65 A; K=1-120.
DR   PDB; 3I4M; X-ray; 3.70 A; K=1-120.
DR   PDB; 3I4N; X-ray; 3.90 A; K=1-120.
DR   PDB; 3J0K; EM; 36.00 A; K=1-120.
DR   PDB; 3J1N; EM; 16.00 A; K=1-120.
DR   PDB; 3K1F; X-ray; 4.30 A; K=1-120.
DR   PDB; 3K7A; X-ray; 3.80 A; K=1-120.
DR   PDB; 3M3Y; X-ray; 3.18 A; K=1-120.
DR   PDB; 3M4O; X-ray; 3.57 A; K=1-120.
DR   PDB; 3PO2; X-ray; 3.30 A; K=1-120.
DR   PDB; 3PO3; X-ray; 3.30 A; K=1-120.
DR   PDB; 3QT1; X-ray; 4.30 A; K=1-120.
DR   PDB; 3RZD; X-ray; 3.30 A; K=1-120.
DR   PDB; 3RZO; X-ray; 3.00 A; K=1-120.
DR   PDB; 3S14; X-ray; 2.85 A; K=1-120.
DR   PDB; 3S15; X-ray; 3.30 A; K=1-120.
DR   PDB; 3S16; X-ray; 3.24 A; K=1-120.
DR   PDB; 3S17; X-ray; 3.20 A; K=1-120.
DR   PDB; 3S1M; X-ray; 3.13 A; K=1-120.
DR   PDB; 3S1N; X-ray; 3.10 A; K=1-120.
DR   PDB; 3S1Q; X-ray; 3.30 A; K=1-120.
DR   PDB; 3S1R; X-ray; 3.20 A; K=1-120.
DR   PDB; 3S2D; X-ray; 3.20 A; K=1-120.
DR   PDB; 3S2H; X-ray; 3.30 A; K=1-120.
DR   PDB; 4A3B; X-ray; 3.50 A; K=1-120.
DR   PDB; 4A3C; X-ray; 3.50 A; K=1-120.
DR   PDB; 4A3D; X-ray; 3.40 A; K=1-120.
DR   PDB; 4A3E; X-ray; 3.40 A; K=1-120.
DR   PDB; 4A3F; X-ray; 3.50 A; K=1-120.
DR   PDB; 4A3G; X-ray; 3.50 A; K=1-120.
DR   PDB; 4A3I; X-ray; 3.80 A; K=1-120.
DR   PDB; 4A3J; X-ray; 3.70 A; K=1-120.
DR   PDB; 4A3K; X-ray; 3.50 A; K=1-120.
DR   PDB; 4A3L; X-ray; 3.50 A; K=1-120.
DR   PDB; 4A3M; X-ray; 3.90 A; K=1-120.
DR   PDB; 4A93; X-ray; 3.40 A; K=1-120.
DR   PDB; 4BBR; X-ray; 3.40 A; K=1-120.
DR   PDB; 4BBS; X-ray; 3.60 A; K=1-120.
DR   PDB; 4BXX; X-ray; 3.28 A; K=1-120.
DR   PDB; 4BXZ; X-ray; 4.80 A; K=1-120.
DR   PDB; 4BY1; X-ray; 3.60 A; K=1-120.
DR   PDB; 4BY7; X-ray; 3.15 A; K=1-120.
DR   PDB; 4V1M; EM; 6.60 A; K=1-120.
DR   PDB; 4V1N; EM; 7.80 A; K=1-120.
DR   PDB; 4V1O; EM; 9.70 A; K=1-120.
DR   PDB; 4X67; X-ray; 4.10 A; K=1-120.
DR   PDB; 4X6A; X-ray; 3.96 A; K=1-120.
DR   PDB; 4Y52; X-ray; 3.50 A; K=1-120.
DR   PDB; 4Y7N; X-ray; 3.30 A; K=1-120.
DR   PDB; 5C3E; X-ray; 3.70 A; K=1-120.
DR   PDB; 5C44; X-ray; 3.95 A; K=1-120.
DR   PDB; 5C4A; X-ray; 4.20 A; K=1-120.
DR   PDB; 5C4J; X-ray; 4.00 A; K=1-120.
DR   PDB; 5C4X; X-ray; 4.00 A; K=1-120.
DR   PDB; 5FMF; EM; 6.00 A; K=1-115.
DR   PDB; 5FYW; EM; 4.35 A; K=1-120.
DR   PDB; 5FZ5; EM; 8.80 A; K=1-120.
DR   PDB; 5IP7; X-ray; 3.52 A; K=1-115.
DR   PDB; 5IP9; X-ray; 3.90 A; K=1-115.
DR   PDB; 5OQJ; EM; 4.70 A; K=1-120.
DR   PDB; 5OQM; EM; 5.80 A; K=1-120.
DR   PDB; 5OT2; X-ray; 3.20 A; K=1-120.
DR   PDB; 5SVA; EM; 15.30 A; K=1-120.
DR   PDB; 5U5Q; X-ray; 3.80 A; K=1-120.
DR   PDB; 5VVR; EM; 5.80 A; K=1-120.
DR   PDB; 5VVS; EM; 6.40 A; K=1-120.
DR   PDB; 5W4U; X-ray; 3.60 A; K=1-120.
DR   PDB; 5W51; X-ray; 3.40 A; K=1-120.
DR   PDB; 6BLO; X-ray; 3.40 A; K=1-120.
DR   PDB; 6BLP; X-ray; 3.20 A; K=1-120.
DR   PDB; 6BM2; X-ray; 3.40 A; K=1-120.
DR   PDB; 6BM4; X-ray; 2.95 A; K=1-120.
DR   PDB; 6BQF; X-ray; 3.35 A; K=1-120.
DR   PDB; 6GYK; EM; 5.10 A; K=1-120.
DR   PDB; 6GYL; EM; 4.80 A; K=1-120.
DR   PDB; 6GYM; EM; 6.70 A; K=1-120.
DR   PDB; 6I84; EM; 4.40 A; K=1-120.
DR   PDB; 6O6C; EM; 3.10 A; I=1-120.
DR   PDB; 6UPX; X-ray; 3.40 A; K=1-120.
DR   PDB; 6UPY; X-ray; 3.40 A; K=1-120.
DR   PDB; 6UPZ; X-ray; 3.10 A; K=1-120.
DR   PDB; 6UQ0; X-ray; 3.56 A; K=1-120.
DR   PDB; 6UQ1; X-ray; 3.60 A; K=1-120.
DR   PDB; 6UQ2; X-ray; 3.20 A; K=1-120.
DR   PDB; 6UQ3; X-ray; 3.47 A; K=1-120.
DR   PDB; 7KED; X-ray; 3.60 A; K=1-120.
DR   PDB; 7KEE; X-ray; 3.45 A; K=1-120.
DR   PDB; 7KEF; X-ray; 3.89 A; K=1-120.
DR   PDB; 7NKX; EM; 2.90 A; K=1-120.
DR   PDB; 7NKY; EM; 3.20 A; K=1-120.
DR   PDB; 7O4I; EM; 3.20 A; K=1-120.
DR   PDB; 7O4J; EM; 2.90 A; K=1-120.
DR   PDB; 7O72; EM; 3.40 A; K=1-120.
DR   PDB; 7O73; EM; 3.40 A; K=1-120.
DR   PDB; 7O75; EM; 3.20 A; K=1-120.
DR   PDB; 7RIM; X-ray; 2.90 A; K=1-120.
DR   PDB; 7RIP; X-ray; 3.30 A; K=1-120.
DR   PDB; 7RIQ; X-ray; 3.00 A; K=1-120.
DR   PDB; 7RIW; X-ray; 3.20 A; K=1-120.
DR   PDB; 7RIX; X-ray; 3.40 A; K=1-120.
DR   PDB; 7RIY; X-ray; 3.70 A; K=1-120.
DR   PDBsum; 1I3Q; -.
DR   PDBsum; 1I50; -.
DR   PDBsum; 1I6H; -.
DR   PDBsum; 1K83; -.
DR   PDBsum; 1NIK; -.
DR   PDBsum; 1NT9; -.
DR   PDBsum; 1PQV; -.
DR   PDBsum; 1R5U; -.
DR   PDBsum; 1R9S; -.
DR   PDBsum; 1R9T; -.
DR   PDBsum; 1SFO; -.
DR   PDBsum; 1TWA; -.
DR   PDBsum; 1TWC; -.
DR   PDBsum; 1TWF; -.
DR   PDBsum; 1TWG; -.
DR   PDBsum; 1TWH; -.
DR   PDBsum; 1WCM; -.
DR   PDBsum; 1Y1V; -.
DR   PDBsum; 1Y1W; -.
DR   PDBsum; 1Y1Y; -.
DR   PDBsum; 1Y77; -.
DR   PDBsum; 2B63; -.
DR   PDBsum; 2B8K; -.
DR   PDBsum; 2E2H; -.
DR   PDBsum; 2E2I; -.
DR   PDBsum; 2E2J; -.
DR   PDBsum; 2JA5; -.
DR   PDBsum; 2JA6; -.
DR   PDBsum; 2JA7; -.
DR   PDBsum; 2JA8; -.
DR   PDBsum; 2NVQ; -.
DR   PDBsum; 2NVT; -.
DR   PDBsum; 2NVX; -.
DR   PDBsum; 2NVY; -.
DR   PDBsum; 2NVZ; -.
DR   PDBsum; 2R7Z; -.
DR   PDBsum; 2R92; -.
DR   PDBsum; 2R93; -.
DR   PDBsum; 2VUM; -.
DR   PDBsum; 2YU9; -.
DR   PDBsum; 3CQZ; -.
DR   PDBsum; 3FKI; -.
DR   PDBsum; 3GTG; -.
DR   PDBsum; 3GTJ; -.
DR   PDBsum; 3GTK; -.
DR   PDBsum; 3GTL; -.
DR   PDBsum; 3GTM; -.
DR   PDBsum; 3GTO; -.
DR   PDBsum; 3GTP; -.
DR   PDBsum; 3GTQ; -.
DR   PDBsum; 3H3V; -.
DR   PDBsum; 3HOU; -.
DR   PDBsum; 3HOV; -.
DR   PDBsum; 3HOW; -.
DR   PDBsum; 3HOX; -.
DR   PDBsum; 3HOY; -.
DR   PDBsum; 3HOZ; -.
DR   PDBsum; 3I4M; -.
DR   PDBsum; 3I4N; -.
DR   PDBsum; 3J0K; -.
DR   PDBsum; 3J1N; -.
DR   PDBsum; 3K1F; -.
DR   PDBsum; 3K7A; -.
DR   PDBsum; 3M3Y; -.
DR   PDBsum; 3M4O; -.
DR   PDBsum; 3PO2; -.
DR   PDBsum; 3PO3; -.
DR   PDBsum; 3QT1; -.
DR   PDBsum; 3RZD; -.
DR   PDBsum; 3RZO; -.
DR   PDBsum; 3S14; -.
DR   PDBsum; 3S15; -.
DR   PDBsum; 3S16; -.
DR   PDBsum; 3S17; -.
DR   PDBsum; 3S1M; -.
DR   PDBsum; 3S1N; -.
DR   PDBsum; 3S1Q; -.
DR   PDBsum; 3S1R; -.
DR   PDBsum; 3S2D; -.
DR   PDBsum; 3S2H; -.
DR   PDBsum; 4A3B; -.
DR   PDBsum; 4A3C; -.
DR   PDBsum; 4A3D; -.
DR   PDBsum; 4A3E; -.
DR   PDBsum; 4A3F; -.
DR   PDBsum; 4A3G; -.
DR   PDBsum; 4A3I; -.
DR   PDBsum; 4A3J; -.
DR   PDBsum; 4A3K; -.
DR   PDBsum; 4A3L; -.
DR   PDBsum; 4A3M; -.
DR   PDBsum; 4A93; -.
DR   PDBsum; 4BBR; -.
DR   PDBsum; 4BBS; -.
DR   PDBsum; 4BXX; -.
DR   PDBsum; 4BXZ; -.
DR   PDBsum; 4BY1; -.
DR   PDBsum; 4BY7; -.
DR   PDBsum; 4V1M; -.
DR   PDBsum; 4V1N; -.
DR   PDBsum; 4V1O; -.
DR   PDBsum; 4X67; -.
DR   PDBsum; 4X6A; -.
DR   PDBsum; 4Y52; -.
DR   PDBsum; 4Y7N; -.
DR   PDBsum; 5C3E; -.
DR   PDBsum; 5C44; -.
DR   PDBsum; 5C4A; -.
DR   PDBsum; 5C4J; -.
DR   PDBsum; 5C4X; -.
DR   PDBsum; 5FMF; -.
DR   PDBsum; 5FYW; -.
DR   PDBsum; 5FZ5; -.
DR   PDBsum; 5IP7; -.
DR   PDBsum; 5IP9; -.
DR   PDBsum; 5OQJ; -.
DR   PDBsum; 5OQM; -.
DR   PDBsum; 5OT2; -.
DR   PDBsum; 5SVA; -.
DR   PDBsum; 5U5Q; -.
DR   PDBsum; 5VVR; -.
DR   PDBsum; 5VVS; -.
DR   PDBsum; 5W4U; -.
DR   PDBsum; 5W51; -.
DR   PDBsum; 6BLO; -.
DR   PDBsum; 6BLP; -.
DR   PDBsum; 6BM2; -.
DR   PDBsum; 6BM4; -.
DR   PDBsum; 6BQF; -.
DR   PDBsum; 6GYK; -.
DR   PDBsum; 6GYL; -.
DR   PDBsum; 6GYM; -.
DR   PDBsum; 6I84; -.
DR   PDBsum; 6O6C; -.
DR   PDBsum; 6UPX; -.
DR   PDBsum; 6UPY; -.
DR   PDBsum; 6UPZ; -.
DR   PDBsum; 6UQ0; -.
DR   PDBsum; 6UQ1; -.
DR   PDBsum; 6UQ2; -.
DR   PDBsum; 6UQ3; -.
DR   PDBsum; 7KED; -.
DR   PDBsum; 7KEE; -.
DR   PDBsum; 7KEF; -.
DR   PDBsum; 7NKX; -.
DR   PDBsum; 7NKY; -.
DR   PDBsum; 7O4I; -.
DR   PDBsum; 7O4J; -.
DR   PDBsum; 7O72; -.
DR   PDBsum; 7O73; -.
DR   PDBsum; 7O75; -.
DR   PDBsum; 7RIM; -.
DR   PDBsum; 7RIP; -.
DR   PDBsum; 7RIQ; -.
DR   PDBsum; 7RIW; -.
DR   PDBsum; 7RIX; -.
DR   PDBsum; 7RIY; -.
DR   AlphaFoldDB; P38902; -.
DR   SMR; P38902; -.
DR   BioGRID; 34399; 393.
DR   ComplexPortal; CPX-2662; DNA-directed RNA polymerase II complex.
DR   DIP; DIP-937N; -.
DR   IntAct; P38902; 21.
DR   MINT; P38902; -.
DR   STRING; 4932.YOL005C; -.
DR   iPTMnet; P38902; -.
DR   MaxQB; P38902; -.
DR   PaxDb; P38902; -.
DR   PRIDE; P38902; -.
DR   EnsemblFungi; YOL005C_mRNA; YOL005C; YOL005C.
DR   GeneID; 854157; -.
DR   KEGG; sce:YOL005C; -.
DR   SGD; S000005365; RPB11.
DR   VEuPathDB; FungiDB:YOL005C; -.
DR   eggNOG; KOG4392; Eukaryota.
DR   HOGENOM; CLU_090381_2_1_1; -.
DR   InParanoid; P38902; -.
DR   OMA; LEQACTK; -.
DR   BioCyc; YEAST:G3O-33422-MON; -.
DR   Reactome; R-SCE-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR   Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-SCE-6807505; RNA polymerase II transcribes snRNA genes.
DR   Reactome; R-SCE-72086; mRNA Capping.
DR   Reactome; R-SCE-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-SCE-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-SCE-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-SCE-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   Reactome; R-SCE-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
DR   EvolutionaryTrace; P38902; -.
DR   PRO; PR:P38902; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P38902; protein.
DR   GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR   GO; GO:0005665; C:RNA polymerase II, core complex; IDA:SGD.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0001055; F:RNA polymerase II activity; IEA:InterPro.
DR   GO; GO:0006369; P:termination of RNA polymerase II transcription; IMP:SGD.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:ComplexPortal.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR   GO; GO:0001172; P:transcription, RNA-templated; IEA:GOC.
DR   CDD; cd06926; RNAP_II_RPB11; 1.
DR   Gene3D; 3.30.1360.10; -; 1.
DR   HAMAP; MF_00261; RNApol_arch_Rpo11; 1.
DR   InterPro; IPR037685; RBP11.
DR   InterPro; IPR036603; RBP11-like.
DR   InterPro; IPR009025; RBP11-like_dimer.
DR   InterPro; IPR008193; RNA_pol_Rpb11_13-16kDa_CS.
DR   Pfam; PF13656; RNA_pol_L_2; 1.
DR   SUPFAM; SSF55257; SSF55257; 1.
DR   PROSITE; PS01154; RNA_POL_L_13KD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; DNA-directed RNA polymerase;
KW   Nucleus; Reference proteome; Transcription.
FT   CHAIN           1..120
FT                   /note="DNA-directed RNA polymerase II subunit RPB11"
FT                   /id="PRO_0000149315"
FT   MUTAGEN         108
FT                   /note="E->G,V: Transcript termination readthrough."
FT                   /evidence="ECO:0000269|PubMed:16537912"
FT   MUTAGEN         108
FT                   /note="E->K: Transcript termination readthrough. Lethal."
FT                   /evidence="ECO:0000269|PubMed:16537912"
FT   MUTAGEN         111
FT                   /note="L->P: Transcript termination readthrough."
FT                   /evidence="ECO:0000269|PubMed:16537912"
FT   MUTAGEN         114
FT                   /note="L->P: Transcript termination readthrough."
FT                   /evidence="ECO:0000269|PubMed:16537912"
FT   HELIX           7..9
FT                   /evidence="ECO:0007829|PDB:1TWF"
FT   STRAND          18..20
FT                   /evidence="ECO:0007829|PDB:3S2H"
FT   STRAND          21..23
FT                   /evidence="ECO:0007829|PDB:1TWF"
FT   STRAND          25..27
FT                   /evidence="ECO:0007829|PDB:1TWF"
FT   STRAND          30..37
FT                   /evidence="ECO:0007829|PDB:1TWF"
FT   HELIX           40..50
FT                   /evidence="ECO:0007829|PDB:1TWF"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:2VUM"
FT   STRAND          56..62
FT                   /evidence="ECO:0007829|PDB:1TWF"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:3CQZ"
FT   STRAND          70..77
FT                   /evidence="ECO:0007829|PDB:1TWF"
FT   HELIX           83..108
FT                   /evidence="ECO:0007829|PDB:1TWF"
FT   TURN            109..111
FT                   /evidence="ECO:0007829|PDB:1TWF"
SQ   SEQUENCE   120 AA;  13616 MW;  A98D109C5FF8E356 CRC64;
     MNAPDRFELF LLGEGESKLK IDPDTKAPNA VVITFEKEDH TLGNLIRAEL LNDRKVLFAA
     YKVEHPFFAR FKLRIQTTEG YDPKDALKNA CNSIINKLGA LKTNFETEWN LQTLAADDAF
 
 
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