RPB4_YEAST
ID RPB4_YEAST Reviewed; 221 AA.
AC P20433; D6VW44;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB4;
DE Short=RNA polymerase II subunit B4;
DE AltName: Full=B32;
DE AltName: Full=DNA-directed RNA polymerase II 32 kDa polypeptide;
GN Name=RPB4; OrderedLocusNames=YJL140W; ORFNames=J0654;
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].
RX PubMed=2674672; DOI=10.1128/mcb.9.7.2854-2859.1989;
RA Woychik N.A., Young R.A.;
RT "RNA polymerase II subunit RPB4 is essential for high- and low-temperature
RT yeast cell growth.";
RL Mol. Cell. Biol. 9:2854-2859(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2041753; DOI=10.1093/nar/19.10.2781;
RA Foreman P.K., Davis R.W., Sachs A.B.;
RT "The Saccharomyces cerevisiae RPB4 gene is tightly linked to the TIF2
RT gene.";
RL Nucleic Acids Res. 19:2781-2781(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8813765;
RX DOI=10.1002/(sici)1097-0061(19960630)12:8<787::aid-yea954>3.0.co;2-4;
RA Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.;
RT "Sequence analysis of a 40.7 kb segment from the left arm of yeast
RT chromosome X reveals 14 known genes and 13 new open reading frames
RT including homologues of genes clustered on the right arm of chromosome
RT XI.";
RL Yeast 12:787-797(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [5]
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 [6]
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 [7]
RP FUNCTION OF THE RPB4-RPB7 COMPLEX.
RX PubMed=1985924; DOI=10.1016/s0021-9258(18)52403-0;
RA Edwards A.M., Kane C.M., Young R.A., Kornberg R.D.;
RT "Two dissociable subunits of yeast RNA polymerase II stimulate the
RT initiation of transcription at a promoter in vitro.";
RL J. Biol. Chem. 266:71-75(1991).
RN [8]
RP FUNCTION OF THE RPB4-RPB7 COMPLEX.
RX PubMed=11087726; DOI=10.1074/jbc.m003165200;
RA Orlicky S.M., Tran P.T., Sayre M.H., Edwards A.M.;
RT "Dissociable Rpb4-Rpb7 subassembly of RNA polymerase II binds to single-
RT strand nucleic acid and mediates a post-recruitment step in transcription
RT initiation.";
RL J. Biol. Chem. 276:10097-10102(2001).
RN [9]
RP FUNCTION.
RX PubMed=11382749; DOI=10.1074/jbc.m010952200;
RA Pillai B., Sampath V., Sharma N., Sadhale P.;
RT "Rpb4, a non-essential subunit of core RNA polymerase II of Saccharomyces
RT cerevisiae is important for activated transcription of a subset of genes.";
RL J. Biol. Chem. 276:30641-30647(2001).
RN [10]
RP FUNCTION IN DNA REPAIR.
RX PubMed=12411509; DOI=10.1093/emboj/cdf589;
RA Li S., Smerdon M.J.;
RT "Rpb4 and Rpb9 mediate subpathways of transcription-coupled DNA repair in
RT Saccharomyces cerevisiae.";
RL EMBO J. 21:5921-5929(2002).
RN [11]
RP FUNCTION IN MRNA EXPORT.
RX PubMed=12857861; DOI=10.1091/mbc.e02-11-0740;
RA Farago M., Nahari T., Hammel C., Cole C.N., Choder M.;
RT "Rpb4p, a subunit of RNA polymerase II, mediates mRNA export during
RT stress.";
RL Mol. Biol. Cell 14:2744-2755(2003).
RN [12]
RP FUNCTION OF THE RPB4-RPB7 COMPLEX.
RX PubMed=15304220; DOI=10.1016/j.molcel.2004.06.035;
RA Kamenski T., Heilmeier S., Meinhart A., Cramer P.;
RT "Structure and mechanism of RNA polymerase II CTD phosphatases.";
RL Mol. Cell 15:399-407(2004).
RN [13]
RP FUNCTION IN MRNA DECAY, SUBCELLULAR LOCATION, AND INTERACTION WITH PAT1 AND
RP LSM2.
RX PubMed=16357218; DOI=10.1101/gad.353205;
RA Lotan R., Bar-On V.G., Harel-Sharvit L., Duek L., Melamed D., Choder M.;
RT "The RNA polymerase II subunit Rpb4p mediates decay of a specific class of
RT mRNAs.";
RL Genes Dev. 19:3004-3016(2005).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=17056745; DOI=10.1128/ec.00288-06;
RA Selitrennik M., Duek L., Lotan R., Choder M.;
RT "Nucleocytoplasmic shuttling of the Rpb4p and Rpb7p subunits of
RT Saccharomyces cerevisiae RNA polymerase II by two pathways.";
RL Eukaryot. Cell 5:2092-2103(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-91 AND THR-92, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP ELECTRON MICROSCOPY OF THE RNA POL II/TFIIF COMPLEX, AND INTERACTION WITH
RP TFG1.
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 [18]
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 [19]
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 [20]
RP X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS) OF THE RNA POL II COMPLEX.
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 [21]
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 [22]
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 [23]
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. RPB4 is part of a
CC subcomplex with RPB7 that binds to a pocket formed by RPB1, RPB2 and
CC RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems
CC to lock the clamp via RPB7 in the closed conformation thus preventing
CC double-stranded DNA to enter the active site cleft. The RPB4-RPB7
CC subcomplex binds single-stranded DNA and RNA. The RPB4-RPB7 subcomplex
CC is necessary for promoter-directed transcription initiation but is not
CC required for recruitment of Pol II to active preinitiation complexes
CC and seems to be dispensable for transcription elongation and
CC termination. The RPB4-RPB7 subcomplex recruits FCP1 to Pol II. Involved
CC in DNA repair of damage in the transcribed strand. RPB4 is dispensable
CC under optimal growth conditions, but becomes essential during heat or
CC cold shock and under nutrient depletion. Suppresses the RBP9-mediated
CC transcription-coupled repair (TCR) subpathway of nucleotide excision
CC repair (NER) but facilitates the RAD26-mediated TCR subpathway. Under
CC stress conditions only, involved in mRNA export to the cytoplasm.
CC Involved in mRNA decay. Promotes or enhances the deadenylation process
CC of specific mRNAs and may recruit PAT1 and the LSM1-7 complex to these
CC mRNAs, thus stimulating their decapping and further decay.
CC {ECO:0000269|PubMed:11087726, ECO:0000269|PubMed:11382749,
CC ECO:0000269|PubMed:12411509, ECO:0000269|PubMed:12857861,
CC ECO:0000269|PubMed:15304220, ECO:0000269|PubMed:16357218,
CC ECO:0000269|PubMed:1985924}.
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits. RPB4 and RPB7 form a dissociable subcomplex associated
CC with the 10-subunit Pol II core complex. In exponentially proliferating
CC cells, only approximately 20 % of the Pol II complexes contain the
CC RPB4-RPB7 subcomplex. In starving cells, that enter stationary phase,
CC RPB4-RPB7 is associated with Pol II in a stoechiometric manner. The
CC RPB4-RPB7 subcomplex probably associates with TFG1. Interacts with LSM2
CC and PAT1. {ECO:0000269|PubMed:12914699, ECO:0000269|PubMed:14580350,
CC ECO:0000269|PubMed:16341226, ECO:0000269|PubMed:16357218}.
CC -!- INTERACTION:
CC P20433; P32497: NIP1; NbExp=5; IntAct=EBI-15777, EBI-8965;
CC P20433; P34087: RPB7; NbExp=8; IntAct=EBI-15777, EBI-15790;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, P-body. Note=Seems
CC to shuttle between nucleus and cytoplasm in a complex with RPB7.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB4 RNA polymerase subunit
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M27253; AAA34996.1; -; Genomic_DNA.
DR EMBL; X58099; CAA41112.1; -; Genomic_DNA.
DR EMBL; X87371; CAA60815.1; -; Genomic_DNA.
DR EMBL; Z49415; CAA89435.1; -; Genomic_DNA.
DR EMBL; AY557856; AAS56182.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08660.1; -; Genomic_DNA.
DR PIR; A32490; A32490.
DR RefSeq; NP_012395.1; NM_001181573.1.
DR PDB; 1NT9; X-ray; 4.20 A; D=1-221.
DR PDB; 1PQV; X-ray; 3.80 A; D=1-85, D=115-221.
DR PDB; 1WCM; X-ray; 3.80 A; D=4-221.
DR PDB; 1Y14; X-ray; 2.30 A; A/C=35-221.
DR PDB; 1Y1V; X-ray; 3.80 A; D=1-221.
DR PDB; 1Y1W; X-ray; 4.00 A; D=1-221.
DR PDB; 1Y1Y; X-ray; 4.00 A; D=1-221.
DR PDB; 1Y77; X-ray; 4.50 A; D=1-221.
DR PDB; 2B63; X-ray; 3.80 A; D=1-221.
DR PDB; 2B8K; X-ray; 4.15 A; D=1-221.
DR PDB; 2JA5; X-ray; 3.80 A; D=1-221.
DR PDB; 2JA6; X-ray; 4.00 A; D=1-221.
DR PDB; 2JA7; X-ray; 3.80 A; D/P=1-221.
DR PDB; 2JA8; X-ray; 3.80 A; D=1-221.
DR PDB; 2R7Z; X-ray; 3.80 A; D=1-221.
DR PDB; 2R92; X-ray; 3.80 A; D=1-221.
DR PDB; 2R93; X-ray; 4.00 A; D=1-221.
DR PDB; 2VUM; X-ray; 3.40 A; D=1-221.
DR PDB; 3FKI; X-ray; 3.88 A; D=1-221.
DR PDB; 3H3V; X-ray; 4.00 A; E=1-221.
DR PDB; 3HOU; X-ray; 3.20 A; D/P=1-221.
DR PDB; 3HOV; X-ray; 3.50 A; D=1-221.
DR PDB; 3HOW; X-ray; 3.60 A; D=1-221.
DR PDB; 3HOX; X-ray; 3.65 A; D=1-221.
DR PDB; 3HOY; X-ray; 3.40 A; D=1-221.
DR PDB; 3HOZ; X-ray; 3.65 A; D=1-221.
DR PDB; 3I4M; X-ray; 3.70 A; D=1-221.
DR PDB; 3I4N; X-ray; 3.90 A; D=1-221.
DR PDB; 3J0K; EM; 36.00 A; D=1-221.
DR PDB; 3J1N; EM; 16.00 A; D=4-221.
DR PDB; 3K1F; X-ray; 4.30 A; D=1-221.
DR PDB; 3PO2; X-ray; 3.30 A; D=1-221.
DR PDB; 3PO3; X-ray; 3.30 A; D=1-221.
DR PDB; 3QT1; X-ray; 4.30 A; D=3-221.
DR PDB; 4A3B; X-ray; 3.50 A; D=1-221.
DR PDB; 4A3C; X-ray; 3.50 A; D=1-221.
DR PDB; 4A3D; X-ray; 3.40 A; D=1-221.
DR PDB; 4A3E; X-ray; 3.40 A; D=1-221.
DR PDB; 4A3F; X-ray; 3.50 A; D=1-221.
DR PDB; 4A3G; X-ray; 3.50 A; D=1-221.
DR PDB; 4A3I; X-ray; 3.80 A; D=1-221.
DR PDB; 4A3J; X-ray; 3.70 A; D=1-221.
DR PDB; 4A3K; X-ray; 3.50 A; D=1-221.
DR PDB; 4A3L; X-ray; 3.50 A; D=1-221.
DR PDB; 4A3M; X-ray; 3.90 A; D=1-221.
DR PDB; 4A93; X-ray; 3.40 A; D=1-221.
DR PDB; 4BBR; X-ray; 3.40 A; D=1-221.
DR PDB; 4BBS; X-ray; 3.60 A; D=1-221.
DR PDB; 4BXX; X-ray; 3.28 A; D=1-221.
DR PDB; 4BXZ; X-ray; 4.80 A; D=1-221.
DR PDB; 4BY1; X-ray; 3.60 A; D=1-221.
DR PDB; 4BY7; X-ray; 3.15 A; D=1-221.
DR PDB; 4V1N; EM; 7.80 A; D=1-221.
DR PDB; 4V1O; EM; 9.70 A; D=1-221.
DR PDB; 5C3E; X-ray; 3.70 A; D=1-221.
DR PDB; 5C44; X-ray; 3.95 A; D=1-221.
DR PDB; 5C4A; X-ray; 4.20 A; D=1-221.
DR PDB; 5C4X; X-ray; 4.00 A; D=1-221.
DR PDB; 5FMF; EM; 6.00 A; D=3-221.
DR PDB; 5FYW; EM; 4.35 A; D=1-221.
DR PDB; 5FZ5; EM; 8.80 A; D=1-221.
DR PDB; 5IP7; X-ray; 3.52 A; D=1-221.
DR PDB; 5IP9; X-ray; 3.90 A; D=1-221.
DR PDB; 5OQJ; EM; 4.70 A; D=1-221.
DR PDB; 5OQM; EM; 5.80 A; D=1-221.
DR PDB; 5OT2; X-ray; 3.20 A; D=1-221.
DR PDB; 5SVA; EM; 15.30 A; D=1-221.
DR PDB; 5U5Q; X-ray; 3.80 A; D=1-221.
DR PDB; 5VVR; EM; 5.80 A; D=1-221.
DR PDB; 5VVS; EM; 6.40 A; D=1-221.
DR PDB; 6GYK; EM; 5.10 A; D=2-221.
DR PDB; 6GYL; EM; 4.80 A; D=1-221.
DR PDB; 6GYM; EM; 6.70 A; D=1-221.
DR PDB; 6I84; EM; 4.40 A; D=1-221.
DR PDB; 7NKX; EM; 2.90 A; D=1-221.
DR PDB; 7NKY; EM; 3.20 A; D=1-221.
DR PDB; 7O4I; EM; 3.20 A; D=1-221.
DR PDB; 7O4J; EM; 2.90 A; D=1-221.
DR PDB; 7O4K; EM; 3.60 A; D=1-221.
DR PDB; 7O4L; EM; 3.40 A; D=1-221.
DR PDB; 7O72; EM; 3.40 A; D=1-221.
DR PDB; 7O73; EM; 3.40 A; D=1-221.
DR PDB; 7O75; EM; 3.20 A; D=1-221.
DR PDBsum; 1NT9; -.
DR PDBsum; 1PQV; -.
DR PDBsum; 1WCM; -.
DR PDBsum; 1Y14; -.
DR PDBsum; 1Y1V; -.
DR PDBsum; 1Y1W; -.
DR PDBsum; 1Y1Y; -.
DR PDBsum; 1Y77; -.
DR PDBsum; 2B63; -.
DR PDBsum; 2B8K; -.
DR PDBsum; 2JA5; -.
DR PDBsum; 2JA6; -.
DR PDBsum; 2JA7; -.
DR PDBsum; 2JA8; -.
DR PDBsum; 2R7Z; -.
DR PDBsum; 2R92; -.
DR PDBsum; 2R93; -.
DR PDBsum; 2VUM; -.
DR PDBsum; 3FKI; -.
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; 3PO2; -.
DR PDBsum; 3PO3; -.
DR PDBsum; 3QT1; -.
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; 4V1N; -.
DR PDBsum; 4V1O; -.
DR PDBsum; 5C3E; -.
DR PDBsum; 5C44; -.
DR PDBsum; 5C4A; -.
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; 6GYK; -.
DR PDBsum; 6GYL; -.
DR PDBsum; 6GYM; -.
DR PDBsum; 6I84; -.
DR PDBsum; 7NKX; -.
DR PDBsum; 7NKY; -.
DR PDBsum; 7O4I; -.
DR PDBsum; 7O4J; -.
DR PDBsum; 7O4K; -.
DR PDBsum; 7O4L; -.
DR PDBsum; 7O72; -.
DR PDBsum; 7O73; -.
DR PDBsum; 7O75; -.
DR AlphaFoldDB; P20433; -.
DR SMR; P20433; -.
DR BioGRID; 33617; 164.
DR ComplexPortal; CPX-1891; RPB4-RPB7 subcomplex.
DR DIP; DIP-55N; -.
DR IntAct; P20433; 27.
DR MINT; P20433; -.
DR STRING; 4932.YJL140W; -.
DR iPTMnet; P20433; -.
DR MaxQB; P20433; -.
DR PaxDb; P20433; -.
DR PRIDE; P20433; -.
DR EnsemblFungi; YJL140W_mRNA; YJL140W; YJL140W.
DR GeneID; 853301; -.
DR KEGG; sce:YJL140W; -.
DR SGD; S000003676; RPB4.
DR VEuPathDB; FungiDB:YJL140W; -.
DR eggNOG; KOG2351; Eukaryota.
DR GeneTree; ENSGT00390000004912; -.
DR HOGENOM; CLU_110332_0_0_1; -.
DR InParanoid; P20433; -.
DR OMA; EPLHPFE; -.
DR BioCyc; YEAST:G3O-31585-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; P20433; -.
DR PRO; PR:P20433; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P20433; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IDA:SGD.
DR GO; GO:1990328; C:RPB4-RPB7 complex; IPI:ComplexPortal.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0031369; F:translation initiation factor binding; IPI:SGD.
DR GO; GO:0031990; P:mRNA export from nucleus in response to heat stress; IMP:SGD.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IMP:SGD.
DR GO; GO:0045948; P:positive regulation of translational initiation; IMP:SGD.
DR GO; GO:0034402; P:recruitment of 3'-end processing factors to RNA polymerase II holoenzyme complex; 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:SGD.
DR GO; GO:0001172; P:transcription, RNA-templated; IEA:GOC.
DR Gene3D; 1.20.1250.40; -; 1.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR006590; RNA_pol_Rpb4/RPC9_core.
DR InterPro; IPR045222; Rpb4-like.
DR InterPro; IPR005574; Rpb4/RPC9.
DR InterPro; IPR038324; Rpb4/RPC9_sf.
DR PANTHER; PTHR21297; PTHR21297; 1.
DR Pfam; PF03874; RNA_pol_Rpb4; 1.
DR SMART; SM00657; RPOL4c; 1.
DR SUPFAM; SSF47819; SSF47819; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; DNA-directed RNA polymerase;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription.
FT CHAIN 1..221
FT /note="DNA-directed RNA polymerase II subunit RPB4"
FT /id="PRO_0000073984"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..111
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 92
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:3PO2"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:5OT2"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:4BBR"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:7NKY"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1Y14"
FT HELIX 52..71
FT /evidence="ECO:0007829|PDB:1Y14"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:4BXX"
FT HELIX 119..133
FT /evidence="ECO:0007829|PDB:1Y14"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:1Y14"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:1Y14"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:1Y14"
FT HELIX 174..182
FT /evidence="ECO:0007829|PDB:1Y14"
FT HELIX 188..194
FT /evidence="ECO:0007829|PDB:1Y14"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:1Y14"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:1Y14"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:1Y14"
SQ SEQUENCE 221 AA; 25414 MW; 72A8A26871B87775 CRC64;
MNVSTSTFQT RRRRLKKVEE EENAATLQLG QEFQLKQINH QGEEEELIAL NLSEARLVIK
EALVERRRAF KRSQKKHKKK HLKHENANDE TTAVEDEDDD LDEDDVNADD DDFMHSETRE
KELESIDVLL EQTTGGNNKD LKNTMQYLTN FSRFRDQETV GAVIQLLKST GLHPFEVAQL
GSLACDTADE AKTLIPSLNN KISDDELERI LKELSNLETL Y
