P20435 (RPAB2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA-directed RNA polymerases I, II, and III subunit RPABC2
Short name=RNA polymerases I, II, and III subunit ABC2

Alternative name(s):
ABC23
DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide

Gene names

Name:	RPO26
Synonyms:	RPB6
Ordered Locus Names:	YPR187W
ORF Names:	P9677.8

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	155 AA.
Sequence status	Complete.
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. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, RPB6 is part of the clamp element and togther with parts of RPB1 and RPB2 forms a pocket to which the RPB4-RPB7 subcomplex binds By similarity.
Subunit structure	Component of the RNA polymerase I (Pol I), RNA polymerase II (Pol II) and RNA polymerase III (Pol III) complexes consisting of at least 14, 12 and 17 subunits, respectively By similarity. Ref.5 Ref.6 Ref.7
Subcellular location	Cytoplasm. Nucleus Ref.8.
Miscellaneous	Present with 6090 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the archaeal RpoK/eukaryotic RPB6 RNA polymerase subunit family.

Ontologies

Keywords
Biological process	Transcription
Cellular component	Cytoplasm DNA-directed RNA polymerase Nucleus
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	tRNA transcription from RNA polymerase III promoter Inferred from direct assay PubMed 3905793. Source: SGD transcription from RNA polymerase I promoter Inferred from direct assay PubMed 9837969. Source: SGD transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 12697831. Source: SGD
Cellular_component	DNA-directed RNA polymerase I complex Inferred from direct assay PubMed 11486042PubMed 9837969. Source: SGD DNA-directed RNA polymerase II, core complex Inferred from direct assay PubMed 1331084PubMed 2183013Ref.1. Source: SGD DNA-directed RNA polymerase III complex Inferred from direct assay PubMed 10611227PubMed 3905793. Source: SGD cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RPA190	P10964	3	EBI-15786,EBI-15730

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 155

155

DNA-directed RNA polymerases I, II, and III subunit RPABC2

PRO_0000133797

Regions

Region

111 – 132

22

Leucine-zipper

Amino acid modifications

Modified residue

24

1

Phosphoserine Ref.11

Modified residue

82

1

Phosphothreonine Ref.11

Secondary structure

1

.

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155

Helix Strand Turn

Details...

Beta strand

71 – 73

3

Beta strand

76 – 78

3

Helix

87 – 102

16

Helix

117 – 126

10

Beta strand

132 – 137

6

Beta strand

139 – 141

3

Beta strand

143 – 147

5

Turn

148 – 150

3

Sequences

	Sequence		Length	Mass (Da)
	P20435 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: AA3DEF529F94A5E4	FASTA	155	17,910
	10 20 30 40 50 60 MSDYEEAFND GNENFEDFDV EHFSDEETYE EKPQFKDGET TDANGKTIVT GGNGPEDFQQ 70 80 90 100 110 120 HEQIRRKTLK EKAIPKDQRA TTPYMTKYER ARILGTRALQ ISMNAPVFVD LEGETDPLRI 130 140 150 AMKELAEKKI PLVIRRYLPD GSFEDWSVEE LIVDL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Subunits shared by eukaryotic nuclear RNA polymerases." Woychik N.A., Liao S.-M., Kolodziej P.A., Young R.A. Genes Dev. 4:313-323(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A suppressor of an RNA polymerase II mutation of Saccharomyces cerevisiae encodes a subunit common to RNA polymerases I, II, and III." Archambault J., Schappert K.T., Friesen J.D. Mol. Cell. Biol. 10:6123-6131(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Differential roles of phosphorylation in the formation of transcriptional active RNA polymerase I." Fath S., Milkereit P., Peyroche G., Riva M., Carles C., Tschochner H. Proc. Natl. Acad. Sci. U.S.A. 98:14334-14339(2001) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE RNA POL I COMPLEX.
[6]	"Rpa12p, a conserved RNA polymerase I subunit with two functional domains." Van Mullem V., Landrieux E., Vandenhaute J., Thuriaux P. Mol. Microbiol. 43:1105-1113(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE RNA POL I COMPLEX.
[7]	"The A14-A43 heterodimer subunit in yeast RNA pol I and their relationship to Rpb4-Rpb7 pol II subunits." Peyroche G., Levillain E., Siaut M., Callebaut I., Schultz P., Sentenac A., Riva M., Carles C. Proc. Natl. Acad. Sci. U.S.A. 99:14670-14675(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE RNA POL I COMPLEX, INTERACTION WITH RPA43.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"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].
[10]	"The yeast RNA polymerase III transcription machinery: a paradigm for eukaryotic gene activation." Chedin S., Ferri M.L., Peyroche G., Andrau J.-C., Jourdain S., Lefebvre O., Werner M., Carles C., Sentenac A. Cold Spring Harb. Symp. Quant. Biol. 63:381-389(1998) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON THE RNA POL III COMPLEX, PHOSPHORYLATION.
[11]	"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-24 AND THR-82, MASS SPECTROMETRY.
[12]	"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.
[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]	"Structural biology of RNA polymerase III: subcomplex C17/25 X-ray structure and 11 subunit enzyme model." Jasiak A.J., Armache K.J., Martens B., Jansen R.P., Cramer P. Mol. Cell 23:71-81(2006) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF THE POL III CORE COMPLEX.
[24]	"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.
[25]	"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

X53288 Genomic DNA. Translation: CAA37382.1.
M33924 Genomic DNA. Translation: AAA34989.1.
U25841 Genomic DNA. Translation: AAB64616.1.
BK006949 Genomic DNA. Translation: DAA11603.1.

PIR

RNBYR6. S13307.

RefSeq

NP_015513.1. NM_001184284.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I3Q	X-ray	3.10	F	1-155	[»]
1I50	X-ray	2.80	F	1-155	[»]
1I6H	X-ray	3.30	F	1-155	[»]
1K83	X-ray	2.80	F	1-155	[»]
1NIK	X-ray	4.10	F	1-155	[»]
1NT9	X-ray	4.20	F	1-155	[»]
1PQV	X-ray	3.80	F	1-155	[»]
1R5U	X-ray	4.50	F	1-155	[»]
1R9S	X-ray	4.25	F	1-155	[»]
1R9T	X-ray	3.50	F	1-155	[»]
1SFO	X-ray	3.61	F	1-155	[»]
1TWA	X-ray	3.20	F	1-155	[»]
1TWC	X-ray	3.00	F	1-155	[»]
1TWF	X-ray	2.30	F	1-155	[»]
1TWG	X-ray	3.30	F	1-155	[»]
1TWH	X-ray	3.40	F	1-155	[»]
1WCM	X-ray	3.80	F	1-155	[»]
1Y1V	X-ray	3.80	F	1-155	[»]
1Y1W	X-ray	4.00	F	1-155	[»]
1Y1Y	X-ray	4.00	F	1-155	[»]
1Y77	X-ray	4.50	F	1-155	[»]
2B63	X-ray	3.80	F	1-155	[»]
2B8K	X-ray	4.15	F	1-155	[»]
2E2H	X-ray	3.95	F	1-155	[»]
2E2I	X-ray	3.41	F	1-155	[»]
2E2J	X-ray	3.50	F	1-155	[»]
2JA5	X-ray	3.80	F	1-155	[»]
2JA6	X-ray	4.00	F	1-155	[»]
2JA7	X-ray	3.80	F/R	1-155	[»]
2JA8	X-ray	3.80	F	1-155	[»]
2NVQ	X-ray	2.90	F	1-155	[»]
2NVT	X-ray	3.36	F	1-155	[»]
2NVX	X-ray	3.60	F	1-155	[»]
2NVY	X-ray	3.40	F	1-155	[»]
2NVZ	X-ray	4.30	F	1-155	[»]
2R7Z	X-ray	3.80	F	1-155	[»]
2R92	X-ray	3.80	F	1-155	[»]
2R93	X-ray	4.00	F	1-155	[»]
2VUM	X-ray	3.40	F	1-155	[»]
2YU9	X-ray	3.40	F	1-155	[»]
3CQZ	X-ray	2.80	F	1-155	[»]
3FKI	X-ray	3.88	F	1-155	[»]
3GTG	X-ray	3.78	F	1-155	[»]
3GTJ	X-ray	3.42	F	1-155	[»]
3GTK	X-ray	3.80	F	1-155	[»]
3GTL	X-ray	3.38	F	1-155	[»]
3GTM	X-ray	3.80	F	1-155	[»]
3GTO	X-ray	4.00	F	1-155	[»]
3GTP	X-ray	3.90	F	1-155	[»]
3GTQ	X-ray	3.80	F	1-155	[»]
3H3V	X-ray	4.00	G	1-155	[»]
3HOU	X-ray	3.20	F/R	1-155	[»]
3HOV	X-ray	3.50	F	1-155	[»]
3HOW	X-ray	3.60	F	1-155	[»]
3HOX	X-ray	3.65	F	1-155	[»]
3HOY	X-ray	3.40	F	1-155	[»]
3HOZ	X-ray	3.65	F	1-155	[»]
3I4M	X-ray	3.70	F	1-155	[»]
3I4N	X-ray	3.90	F	1-155	[»]
3J1N	electron microscopy	16.00	F	72-155	[»]
3K1F	X-ray	4.30	F	1-155	[»]
3K7A	X-ray	3.80	F	1-155	[»]
3M3Y	X-ray	3.18	F	1-155	[»]
3M4O	X-ray	3.57	F	1-155	[»]
3PO2	X-ray	3.30	F	1-155	[»]
3PO3	X-ray	3.30	F	1-155	[»]
3QT1	X-ray	4.30	F	1-155	[»]
3RZD	X-ray	3.30	F	1-155	[»]
3RZO	X-ray	3.00	F	1-155	[»]
3S14	X-ray	2.85	F	1-155	[»]
3S15	X-ray	3.30	F	1-155	[»]
3S16	X-ray	3.24	F	1-155	[»]
3S17	X-ray	3.20	F	1-155	[»]
3S1M	X-ray	3.13	F	1-155	[»]
3S1N	X-ray	3.10	F	1-155	[»]
3S1Q	X-ray	3.30	F	1-155	[»]
3S1R	X-ray	3.20	F	1-155	[»]
3S2D	X-ray	3.20	F	1-155	[»]
3S2H	X-ray	3.30	F	1-155	[»]
4A3B	X-ray	3.50	F	1-155	[»]
4A3C	X-ray	3.50	F	1-155	[»]
4A3D	X-ray	3.40	F	1-155	[»]
4A3E	X-ray	3.40	F	1-155	[»]
4A3F	X-ray	3.50	F	1-155	[»]
4A3G	X-ray	3.50	F	1-155	[»]
4A3I	X-ray	3.80	F	1-155	[»]
4A3J	X-ray	3.70	F	1-155	[»]
4A3K	X-ray	3.50	F	1-155	[»]
4A3L	X-ray	3.50	F	1-155	[»]
4A3M	X-ray	3.90	F	1-155	[»]
4A93	X-ray	3.40	F	1-155	[»]
4BBR	X-ray	3.40	F	1-155	[»]
4BBS	X-ray	3.60	F	1-155	[»]

ProteinModelPortal

P20435.

SMR

P20435. Positions 72-155.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2194N.

IntAct

P20435. 37 interactions.

MINT

MINT-569579.

STRING

4932.YPR187W.

Proteomic databases

PaxDb

P20435.

PeptideAtlas

P20435.

PRIDE

P20435.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YPR187W; YPR187W; YPR187W.

GeneID

856317.

KEGG

sce:YPR187W.

Organism-specific databases

CYGD

YPR187w.

SGD

S000006391. RPO26.

Phylogenomic databases

eggNOG

COG1758.

GeneTree

ENSGT00390000010415.

HOGENOM

HOG000225272.

KO

K03014.

OMA

EDWSVEE.

OrthoDB

EOG4FR42D.

Enzyme and pathway databases

Reactome

REACT_83470. Gene Expression.
REACT_87991. Transcription.

Gene expression databases

Genevestigator

P20435.

GermOnline

YPR187W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.90.940.10. 1 hit.

InterPro

IPR020708. DNA-dir_RNA_polK_14-18kDa_CS.
IPR006110. RNA_poly_omega/K/RPABC2.
IPR006111. RNAP_K/Rpb6.
IPR012293. RNAP_RPB6_omega.
[Graphical view]

PANTHER

PTHR10773. PTHR10773. 1 hit.

Pfam

PF01192. RNA_pol_Rpb6. 1 hit.
[Graphical view]

PIRSF

PIRSF000778. RpoK/RPB6. 1 hit.

SUPFAM

SSF63562. RNA_pol_omega. 1 hit.

PROSITE

PS01111. RNA_POL_K_14KD. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P20435.

NextBio

981703.

Entry information

Entry name

RPAB2_YEAST

Accession

Primary (citable) accession number: P20435
Secondary accession number(s): D6W4I7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	May 1, 2013
This is version 139 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program