Reviewed, UniProtKB/Swiss-Prot P08518 (RPB2_YEAST)

Names and origin

Protein names

Recommended name:
    DNA-directed RNA polymerase II subunit RPB2
      Short name=RNA polymerase II subunit 2
    EC=2.7.7.6
Alternative name(s):
    DNA-directed RNA polymerase II 140 kDa polypeptide
    B150

Gene names

Name:	RPB2
Synonyms:	RPB150, RPO22
Ordered Locus Names:	YOR151C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1224 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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. Ref.8
Sequence similarities	Belongs to the RNA polymerase beta chain family.

Ontologies

Keywords
Biological process	Transcription
Cellular component	DNA-directed RNA polymerase Nucleus
Domain	Zinc-finger
Ligand	Magnesium Metal-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: SGD
Cellular component	DNA-directed RNA polymerase II, core complex Traceable author statement. Source: SGD mitochondrion Inferred from direct assay. Source: SGD
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activity Traceable author statement. Source: SGD magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct ribonucleoside binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ALG7	P07286	1	EBI-15767,EBI-7852
IWS1	Q06505	1	EBI-15767,EBI-32596
KRE27	P40540	1	EBI-15767,EBI-24977
RNR2	P09938	1	EBI-15767,EBI-15240
RPB3	P16370	1	EBI-15767,EBI-15773
RPB5	P20434	1	EBI-15767,EBI-15781
RPO26	P20435	1	EBI-15767,EBI-15786

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1224

1224

DNA-directed RNA polymerase II subunit RPB2

PRO_0000048091

Regions

Zinc finger

1163 – 1185

23

C4-type

Region

467 – 478

12

Fork loop 1

Sites

Metal binding

837

1

Magnesium; shared with RPB1

Metal binding

1163

1

Zinc

Metal binding

1166

1

Zinc

Metal binding

1182

1

Zinc

Metal binding

1185

1

Zinc

Amino acid modifications

Modified residue

915

1

Phosphothreonine Ref.6

Modified residue

916

1

Phosphothreonine Ref.6

Modified residue

919

1

Phosphoserine Ref.6 Ref.10

Experimental info

Sequence conflict

1003 – 1006

4

AEGI → RRRY in AAA68096. Ref.1

Secondary structure

1

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1224

Helix Strand Turn

Details...

Helix

29 – 41

13

Helix

45 – 56

12

Helix

58 – 64

7

Beta strand

96 – 102

7

Beta strand

105 – 107

3

Beta strand

109 – 111

3

Helix

114 – 119

6

Beta strand

125 – 129

5

Beta strand

166 – 171

6

Helix

180 – 182

3

Helix

186 – 191

6

Beta strand

202 – 205

4

Beta strand

208 – 212

5

Beta strand

214 – 218

5

Beta strand

224 – 227

4

Beta strand

232 – 241

10

Beta strand

245 – 247

3

Beta strand

253 – 260

8

Beta strand

269 – 272

4

Helix

282 – 288

7

Helix

294 – 301

8

Helix

308 – 320

13

Turn

321 – 323

3

Helix

327 – 336

10

Helix

345 – 358

14

Turn

362 – 364

3

Beta strand

367 – 369

3

Helix

371 – 389

19

Helix

401 – 403

3

Beta strand

404 – 407

4

Helix

409 – 433

25

Helix

451 – 463

13

Beta strand

480 – 482

3

Helix

488 – 495

8

Beta strand

497 – 499

3

Helix

516 – 518

3

Turn

519 – 521

3

Helix

530 – 532

3

Beta strand

536 – 539

4

Helix

552 – 560

9

Helix

566 – 568

3

Helix

571 – 573

3

Beta strand

578 – 582

5

Beta strand

585 – 591

7

Helix

593 – 606

14

Beta strand

607 – 609

3

Beta strand

614 – 618

5

Turn

619 – 622

4

Beta strand

623 – 627

5

Beta strand

633 – 641

9

Beta strand

650 – 652

3

Helix

655 – 666

12

Helix

681 – 686

6

Beta strand

689 – 694

6

Helix

695 – 698

4

Beta strand

703 – 706

4

Helix

707 – 710

4

Helix

745 – 748

4

Helix

753 – 755

3

Beta strand

756 – 758

3

Helix

759 – 761

3

Helix

764 – 773

10

Helix

774 – 776

3

Turn

783 – 787

5

Beta strand

791 – 798

8

Beta strand

803 – 805

3

Helix

809 – 812

4

Turn

813 – 816

4

Beta strand

821 – 827

7

Beta strand

829 – 832

4

Turn

833 – 837

5

Beta strand

838 – 842

5

Helix

843 – 847

5

Turn

848 – 851

4

Beta strand

853 – 861

9

Beta strand

873 – 875

3

Beta strand

880 – 882

3

Helix

890 – 892

3

Beta strand

910 – 912

3

Beta strand

947 – 956

10

Beta strand

958 – 960

3

Beta strand

962 – 972

11

Beta strand

979 – 981

3

Beta strand

987 – 994

8

Turn

996 – 998

3

Beta strand

1009 – 1012

4

Helix

1014 – 1016

3

Turn

1018 – 1021

4

Helix

1023 – 1038

16

Beta strand

1046 – 1049

4

Helix

1052 – 1060

9

Turn

1061 – 1063

3

Beta strand

1068 – 1070

3

Turn

1075 – 1077

3

Beta strand

1085 – 1097

13

Helix

1099 – 1101

3

Beta strand

1104 – 1106

3

Helix

1132 – 1141

10

Helix

1144 – 1151

8

Beta strand

1159 – 1166

8

Beta strand

1172 – 1174

3

Turn

1175 – 1178

4

Beta strand

1179 – 1182

4

Turn

1183 – 1186

4

Beta strand

1187 – 1195

9

Helix

1198 – 1209

12

Beta strand

1215 – 1218

4

Sequences

	Sequence		Length	Mass (Da)
	P08518-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: BABD03212C0A583E	FASTA	1,224	138,751
	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

References

	« Hide 'large scale' referencesShow '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: 3547406] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 9046089] [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. , 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: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: S288c / FY1678.
[4]	"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: 12748053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 549-773. Strain: ATCC 18824 / CBS 1171 / DSM 70449 / IFO 10217 / NRRL Y-12632.
[5]	"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: 2204624] [Abstract] Cited for: PROTEIN SEQUENCE OF 837-844.
[6]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-915; THR-916 AND SER-919, MASS SPECTROMETRY.
[7]	"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: 14580350] [Abstract] Cited for: ELECTRON MICROSCOPY OF THE RNA POL II/TFIIF COMPLEX.
[8]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"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: 15565157] [Abstract] Cited for: INTERACTION WITH RTT103.
[10]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-919, MASS SPECTROMETRY.
[11]	"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: 11313498] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
[12]	"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: 11313499] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
[13]	"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: 11805306] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE RNA POL II CORE COMPLEX IN COMPLEX WITH ALPHA-AMANITIN.
[14]	"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: 12914699] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX IN COMPLEX WITH DST1.
[15]	"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: 12746495] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS) OF THE RNA POL II COMPLEX.
[16]	"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: 12746498] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
[17]	"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: 15537538] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
[18]	"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: 15610738] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS).
[19]	"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: 14963322] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
[20]	"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: 15591044] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX.
[21]	"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: 16341226] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX IN COMPLEX WITH INHIBITING NON-CODING RNA.
[22]	"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: 16765890] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.15 ANGSTROMS) OF THE RNA POL II COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M15693 Genomic DNA. Translation: AAA68096.1.
U55020 Genomic DNA. Translation: AAC49637.1.
Z75059 Genomic DNA. Translation: CAA99357.1.
AF527884 Genomic DNA. Translation: AAP57849.1.

PIR

A25884.

RefSeq

NP_014794.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I3Q	X-ray	3.10	B	1-1224	[»]
1I50	X-ray	2.80	B	1-1224	[»]
1I6H	X-ray	3.30	B	1-1224	[»]
1K83	X-ray	2.80	B	1-1224	[»]
1NIK	X-ray	4.10	B	1-1224	[»]
1NT9	X-ray	4.20	B	1-1224	[»]
1PQV	X-ray	3.80	B	1-1224	[»]
1R5U	X-ray	4.50	B	1-1224	[»]
1R9S	X-ray	4.25	B	1-1224	[»]
1R9T	X-ray	3.50	B	1-1224	[»]
1SFO	X-ray	3.61	B	1-1224	[»]
1TWA	X-ray	3.20	B	1-1224	[»]
1TWC	X-ray	3.00	B	1-1224	[»]
1TWF	X-ray	2.30	B	1-1224	[»]
1TWG	X-ray	3.30	B	1-1224	[»]
1TWH	X-ray	3.40	B	1-1224	[»]
1WCM	X-ray	3.80	B	1-1224	[»]
1Y1V	X-ray	3.80	B	1-1224	[»]
1Y1W	X-ray	4.00	B	1-1224	[»]
1Y1Y	X-ray	4.00	B	1-1224	[»]
1Y77	X-ray	4.50	B	1-1224	[»]
2B63	X-ray	3.80	B	1-1224	[»]
2B8K	X-ray	4.15	B	1-1224	[»]
2E2H	X-ray	3.95	B	1-1224	[»]
2E2I	X-ray	3.41	B	1-1224	[»]
2E2J	X-ray	3.50	B	1-1224	[»]
2JA5	X-ray	3.80	B	1-1224	[»]
2JA6	X-ray	4.00	B	1-1224	[»]
2JA7	X-ray	3.80	B/N	1-1224	[»]
2JA8	X-ray	3.80	B	1-1224	[»]
2NVQ	X-ray	2.90	B	1-1224	[»]
2NVT	X-ray	3.36	B	1-1224	[»]
2NVX	X-ray	3.60	B	1-1224	[»]
2NVY	X-ray	3.40	B	1-1224	[»]
2NVZ	X-ray	4.30	B	1-1224	[»]
2R7Z	X-ray	3.80	B	1-1224	[»]
2R92	X-ray	3.80	B	1-1224	[»]
2R93	X-ray	4.00	B	1-1224	[»]
2VUM	X-ray	3.40	B	1-1224	[»]
2YU9	X-ray	3.40	B	1-1224	[»]
3CQZ	X-ray	2.80	B	1-1224	[»]
3FKI	X-ray	3.88	B	1-1224	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:14N.

IntAct

P08518. 54 interactions.

Proteomic databases

PeptideAtlas

P08518.

PRIDE

P08518.

Genome annotation databases

Ensembl

YOR151C. Saccharomyces cerevisiae. [Contig view]

GeneID

854322.

GenomeReviews

Gene locus YOR151C in contig Y13140_GR.

KEGG

sce:YOR151C.

NMPDR

fig|4932.3.peg.5899.

Organism-specific databases

CYGD

YOR151c.

SGD

S000005677. RPB2.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P08518.

OMA

P08518. FGPTYYQ.

Enzyme and pathway databases

BRENDA

2.7.7.6. 250.

Gene expression databases

ArrayExpress

P08518.

GermOnline

YOR151C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR015712. 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.
[Graphical view]

PANTHER

PTHR20856. RNA_pol_I_sub2. 1 hit.

Pfam

PF04563. 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]

PROSITE

PS01166. RNA_POL_BETA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

976360.

Entry information

Entry name

RPB2_YEAST

Accession

Primary (citable) accession number: P08518
Secondary accession number(s): Q12738, Q7Z9Y0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)