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P08518 (RPB2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA-directed RNA polymerase II subunit RPB2

Short name=RNA polymerase II subunit 2
EC=2.7.7.6
Alternative name(s):
B150
DNA-directed RNA polymerase II 140 kDa polypeptide
Gene names
Name:RPB2
Synonyms:RPB150, RPO22
Ordered Locus Names:YOR151C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1224 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest component of RNA polymerases II which synthesizes mRNA precursors and many functional non-coding RNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the 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. 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. The cleft is surrounded by jaws: an upper jaw formed by portions of RBP1, RPB2 and RPB9, and a lower jaw. The jaws are thought to grab the incoming DNA template. The fork loop 1 (RPB2) interacts with the RNA-DNA hybrid, possibly stabilizing it.

Catalytic activity

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

Subunit structure

Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits.

Subcellular location

Nucleus.

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 coordinated by three conserved aspartate residues of the two largest RNA Pol II subunits.

Present with 18700 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the RNA polymerase beta chain family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RPB3P163705EBI-15767,EBI-15773
RPB5P204348EBI-15767,EBI-15781

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12241224DNA-directed RNA polymerase II subunit RPB2
PRO_0000048091

Regions

Zinc finger1163 – 118523C4-type
Region467 – 47812Fork loop 1

Sites

Metal binding8371Magnesium; shared with RPB1
Metal binding11631Zinc
Metal binding11661Zinc
Metal binding11821Zinc
Metal binding11851Zinc

Amino acid modifications

Modified residue9191Phosphoserine Ref.7 Ref.8

Experimental info

Sequence conflict1003 – 10064AEGI → RRRY in AAA68096. Ref.1

Secondary structure

.......................................................................................................................................................................................................................................................... 1224
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08518 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: BABD03212C0A583E

FASTA1,224138,751
        10         20         30         40         50         60 
MSDLANSEKY YDEDPYGFED ESAPITAEDS WAVISAFFRE KGLVSQQLDS FNQFVDYTLQ 

        70         80         90        100        110        120 
DIICEDSTLI LEQLAQHTTE SDNISRKYEI SFGKIYVTKP MVNESDGVTH ALYPQEARLR 

       130        140        150        160        170        180 
NLTYSSGLFV DVKKRTYEAI DVPGRELKYE LIAEESEDDS ESGKVFIGRL PIMLRSKNCY 

       190        200        210        220        230        240 
LSEATESDLY KLKECPFDMG GYFIINGSEK VLIAQERSAG NIVQVFKKAA PSPISHVAEI 

       250        260        270        280        290        300 
RSALEKGSRF ISTLQVKLYG REGSSARTIK ATLPYIKQDI PIVIIFRALG IIPDGEILEH 

       310        320        330        340        350        360 
ICYDVNDWQM LEMLKPCVED GFVIQDRETA LDFIGRRGTA LGIKKEKRIQ YAKDILQKEF 

       370        380        390        400        410        420 
LPHITQLEGF ESRKAFFLGY MINRLLLCAL DRKDQDDRDH FGKKRLDLAG PLLAQLFKTL 

       430        440        450        460        470        480 
FKKLTKDIFR YMQRTVEEAH DFNMKLAINA KTITSGLKYA LATGNWGEQK KAMSSRAGVS 

       490        500        510        520        530        540 
QVLNRYTYSS TLSHLRRTNT PIGRDGKLAK PRQLHNTHWG LVCPAETPEG QACGLVKNLS 

       550        560        570        580        590        600 
LMSCISVGTD PMPIITFLSE WGMEPLEDYV PHQSPDATRV FVNGVWHGVH RNPARLMETL 

       610        620        630        640        650        660 
RTLRRKGDIN PEVSMIRDIR EKELKIFTDA GRVYRPLFIV EDDESLGHKE LKVRKGHIAK 

       670        680        690        700        710        720 
LMATEYQDIE GGFEDVEEYT WSSLLNEGLV EYIDAEEEES ILIAMQPEDL EPAEANEEND 

       730        740        750        760        770        780 
LDVDPAKRIR VSHHATTFTH CEIHPSMILG VAASIIPFPD HNQSPRNTYQ SAMGKQAMGV 

       790        800        810        820        830        840 
FLTNYNVRMD TMANILYYPQ KPLGTTRAME YLKFRELPAG QNAIVAIACY SGYNQEDSMI 

       850        860        870        880        890        900 
MNQSSIDRGL FRSLFFRSYM DQEKKYGMSI TETFEKPQRT NTLRMKHGTY DKLDDDGLIA 

       910        920        930        940        950        960 
PGVRVSGEDV IIGKTTPISP DEEELGQRTA YHSKRDASTP LRSTENGIVD QVLVTTNQDG 

       970        980        990       1000       1010       1020 
LKFVKVRVRT TKIPQIGDKF ASRHGQKGTI GITYRREDMP FTAEGIVPDL IINPHAIPSR 

      1030       1040       1050       1060       1070       1080 
MTVAHLIECL LSKVAALSGN EGDASPFTDI TVEGISKLLR EHGYQSRGFE VMYNGHTGKK 

      1090       1100       1110       1120       1130       1140 
LMAQIFFGPT YYQRLRHMVD DKIHARARGP MQVLTRQPVE GRSRDGGLRF GEMERDCMIA 

      1150       1160       1170       1180       1190       1200 
HGAASFLKER LMEASDAFRV HICGICGLMT VIAKLNHNQF ECKGCDNKID IYQIHIPYAA 

      1210       1220 
KLLFQELMAM NITPRLYTDR SRDF 

« Hide

References

« Hide 'large scale' references
[1]"Prokaryotic and eukaryotic RNA polymerases have homologous core subunits."
Sweetser D., Nonet M., Young R.A.
Proc. Natl. Acad. Sci. U.S.A. 84:1192-1196(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"Analysis of a 35.6 kb region on the right arm of Saccharomyces cerevisiae chromosome XV."
Bordonne R., Camasses A., Madania A., Poch O., Tarassov I.A., Winsor B., Martin R.P.
Yeast 13:73-83(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: S288c / FY1678.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Phylogenetic relationships among yeasts of the 'Saccharomyces complex' determined from multigene sequence analyses."
Kurtzman C.P., Robnett C.J.
FEMS Yeast Res. 3:417-432(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 549-773.
Strain: ATCC 18824 / CBS 1171 / DSM 70449 / IFO 10217 / NRRL Y-12632.
[6]"Mapping the active site of yeast RNA polymerase B (II)."
Riva M., Carles C., Sentenac A., Grachev M.A., Mustaev A.A., Zaychikov E.F.
J. Biol. Chem. 265:16498-16503(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 837-844.
[7]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-919, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[8]"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 SER-919, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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.
[11]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]"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).
[21]"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.
[22]"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.
[23]"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.
[24]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15693 Genomic DNA. Translation: AAA68096.1.
U55020 Genomic DNA. Translation: AAC49637.1.
Z75059 Genomic DNA. Translation: CAA99357.1.
AF527884 Genomic DNA. Translation: AAP57849.1.
BK006948 Genomic DNA. Translation: DAA10924.1.
PIRA25884.
RefSeqNP_014794.3. NM_001183570.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I3QX-ray3.10B1-1224[»]
1I50X-ray2.80B1-1224[»]
1I6HX-ray3.30B1-1224[»]
1K83X-ray2.80B1-1224[»]
1NIKX-ray4.10B1-1224[»]
1NT9X-ray4.20B1-1224[»]
1PQVX-ray3.80B1-1224[»]
1R5UX-ray4.50B1-1224[»]
1R9SX-ray4.25B1-1224[»]
1R9TX-ray3.50B1-1224[»]
1SFOX-ray3.61B1-1224[»]
1TWAX-ray3.20B1-1224[»]
1TWCX-ray3.00B1-1224[»]
1TWFX-ray2.30B1-1224[»]
1TWGX-ray3.30B1-1224[»]
1TWHX-ray3.40B1-1224[»]
1WCMX-ray3.80B1-1224[»]
1Y1VX-ray3.80B1-1224[»]
1Y1WX-ray4.00B1-1224[»]
1Y1YX-ray4.00B1-1224[»]
1Y77X-ray4.50B1-1224[»]
2B63X-ray3.80B1-1224[»]
2B8KX-ray4.15B1-1224[»]
2E2HX-ray3.95B1-1224[»]
2E2IX-ray3.41B1-1224[»]
2E2JX-ray3.50B1-1224[»]
2JA5X-ray3.80B1-1224[»]
2JA6X-ray4.00B1-1224[»]
2JA7X-ray3.80B/N1-1224[»]
2JA8X-ray3.80B1-1224[»]
2NVQX-ray2.90B1-1224[»]
2NVTX-ray3.36B1-1224[»]
2NVXX-ray3.60B1-1224[»]
2NVYX-ray3.40B1-1224[»]
2NVZX-ray4.30B1-1224[»]
2R7ZX-ray3.80B1-1224[»]
2R92X-ray3.80B1-1224[»]
2R93X-ray4.00B1-1224[»]
2VUMX-ray3.40B1-1224[»]
2YU9X-ray3.40B1-1224[»]
3CQZX-ray2.80B1-1223[»]
3FKIX-ray3.88B1-1224[»]
3GTGX-ray3.78B1-1224[»]
3GTJX-ray3.42B1-1224[»]
3GTKX-ray3.80B1-1224[»]
3GTLX-ray3.38B1-1224[»]
3GTMX-ray3.80B1-1224[»]
3GTOX-ray4.00B1-1224[»]
3GTPX-ray3.90B1-1224[»]
3GTQX-ray3.80B1-1224[»]
3H3VX-ray4.00C1-1224[»]
3HOUX-ray3.20B/N1-1224[»]
3HOVX-ray3.50B1-1224[»]
3HOWX-ray3.60B1-1224[»]
3HOXX-ray3.65B1-1224[»]
3HOYX-ray3.40B1-1224[»]
3HOZX-ray3.65B1-1224[»]
3I4MX-ray3.70B1-1224[»]
3I4NX-ray3.90B1-1224[»]
3J0Kelectron microscopy36.00B1-1224[»]
3J1Nelectron microscopy16.00B1-1224[»]
3K1FX-ray4.30B1-1224[»]
3K7AX-ray3.80B1-1224[»]
3M3YX-ray3.18B1-1224[»]
3M4OX-ray3.57B1-1224[»]
3PO2X-ray3.30B1-1224[»]
3PO3X-ray3.30B1-1224[»]
3QT1X-ray4.30B1-1224[»]
3RZDX-ray3.30B1-1224[»]
3RZOX-ray3.00B1-1224[»]
3S14X-ray2.85B1-1224[»]
3S15X-ray3.30B1-1224[»]
3S16X-ray3.24B1-1224[»]
3S17X-ray3.20B1-1224[»]
3S1MX-ray3.13B1-1224[»]
3S1NX-ray3.10B1-1224[»]
3S1QX-ray3.30B1-1224[»]
3S1RX-ray3.20B1-1224[»]
3S2DX-ray3.20B1-1224[»]
3S2HX-ray3.30B1-1224[»]
4A3BX-ray3.50B1-1224[»]
4A3CX-ray3.50B1-1224[»]
4A3DX-ray3.40B1-1224[»]
4A3EX-ray3.40B1-1224[»]
4A3FX-ray3.50B1-1224[»]
4A3GX-ray3.50B1-1224[»]
4A3IX-ray3.80B1-1224[»]
4A3JX-ray3.70B1-1224[»]
4A3KX-ray3.50B1-1224[»]
4A3LX-ray3.50B1-1224[»]
4A3MX-ray3.90B1-1224[»]
4A93X-ray3.40B1-1224[»]
4BBRX-ray3.40B1-1224[»]
4BBSX-ray3.60B1-1224[»]
4BXXX-ray3.28B1-1224[»]
4BXZX-ray4.80B1-1224[»]
4BY1X-ray3.60B1-1224[»]
4BY7X-ray3.15B1-1224[»]
ProteinModelPortalP08518.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34547. 135 interactions.
DIPDIP-14N.
IntActP08518. 62 interactions.
MINTMINT-654304.

Proteomic databases

MaxQBP08518.
PaxDbP08518.
PeptideAtlasP08518.
PRIDEP08518.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR151C; YOR151C; YOR151C.
GeneID854322.
KEGGsce:YOR151C.

Organism-specific databases

CYGDYOR151c.
SGDS000005677. RPB2.

Phylogenomic databases

eggNOGCOG0085.
GeneTreeENSGT00750000117589.
HOGENOMHOG000222962.
KOK03010.
OMADSQMLEM.
OrthoDBEOG7RRFGC.

Enzyme and pathway databases

BioCycYEAST:G3O-33668-MONOMER.

Gene expression databases

GenevestigatorP08518.

Family and domain databases

Gene3D2.40.270.10. 2 hits.
2.40.50.150. 1 hit.
3.90.1110.10. 1 hit.
InterProIPR015712. DNA-dir_RNA_pol_su2.
IPR007120. DNA-dir_RNA_pol_su2_6.
IPR007121. RNA_pol_bsu_CS.
IPR007644. RNA_pol_bsu_protrusion.
IPR007642. RNA_pol_Rpb2_2.
IPR007645. RNA_pol_Rpb2_3.
IPR007646. RNA_pol_Rpb2_4.
IPR007647. RNA_pol_Rpb2_5.
IPR007641. RNA_pol_Rpb2_7.
IPR014724. RNA_pol_RPB2_OB-fold.
[Graphical view]
PANTHERPTHR20856. PTHR20856. 1 hit.
PfamPF04563. RNA_pol_Rpb2_1. 1 hit.
PF04561. RNA_pol_Rpb2_2. 1 hit.
PF04565. RNA_pol_Rpb2_3. 1 hit.
PF04566. RNA_pol_Rpb2_4. 1 hit.
PF04567. RNA_pol_Rpb2_5. 1 hit.
PF00562. RNA_pol_Rpb2_6. 1 hit.
PF04560. RNA_pol_Rpb2_7. 1 hit.
[Graphical view]
PROSITEPS01166. RNA_POL_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08518.
NextBio976360.
PROP08518.

Entry information

Entry nameRPB2_YEAST
AccessionPrimary (citable) accession number: P08518
Secondary accession number(s): D6W2K8, Q12738, Q7Z9Y0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references