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P20434 (RPAB1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. 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 polymerases I, II, and III subunit RPABC1

Short name=RNA polymerases I, II, and III subunit ABC1
Alternative name(s):
ABC27
DNA-directed RNA polymerases I, II, and III 27 kDa polypeptide
Gene names
Name:RPB5
Synonyms:RPA7, RPC9
Ordered Locus Names:YBR154C
ORF Names:YBR1204
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA-dependent RNA polymerases catalyze 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. RNA polymerase complexes are composed of mobile elements that move relative to each other. In Pol II, RPB5 is part of the lower jaw surrounding the central large cleft and thought to grab the incoming DNA template. Seems to be the major component in this process. Ref.24 Ref.25 Ref.26

Subunit structure

Component of the RNA polymerase I (Pol I), RNA polymerase II (Pol II) and RNA polymerase III (Pol III) complexes. Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that mediates interactions with transcription initiation factors and newly synthesized RNA. Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits: RPO21, RPB2, RPB3, RPB4, RPB5, RPO26, RPB7, RPB8, RPB9, RPB10 and RPC10. Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. Ref.6 Ref.7 Ref.8 Ref.24 Ref.25 Ref.26

Subcellular location

Nucleus HAMAP-Rule MF_00025.

Sequence similarities

Belongs to the archaeal RpoH/eukaryotic RPB5 RNA polymerase subunit family.

Ontologies

Keywords
   Biological processRibosome biogenesis
Transcription
   Cellular componentDNA-directed RNA polymerase
Nucleus
   LigandDNA-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processribosome biogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

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 Ref.25. Source: UniProtKB

transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 17179178PubMed 9860960. Source: SGD

transcription from RNA polymerase III promoter

Inferred from mutant phenotype PubMed 17179178. Source: SGD

transcription, RNA-templated

Inferred from direct assay PubMed 18004386. Source: GOC

   Cellular_componentDNA-directed RNA polymerase I complex

Inferred from direct assay Ref.25. Source: UniProtKB

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

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase I activity

Inferred from direct assay Ref.25. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16429126PubMed 18467557PubMed 20094031PubMed 21386817PubMed 22056778. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RPB2P085188EBI-15781,EBI-15767

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 215215DNA-directed RNA polymerases I, II, and III subunit RPABC1 HAMAP-Rule MF_00025
PRO_0000146086

Experimental info

Sequence conflict371L → W in AAC60556. Ref.2

Secondary structure

..................................................... 215
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20434 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 2A15F7114D69D829

FASTA21525,079
        10         20         30         40         50         60 
MDQENERNIS RLWRAFRTVK EMVKDRGYFI TQEEVELPLE DFKAKYCDSM GRPQRKMMSF 

        70         80         90        100        110        120 
QANPTEESIS KFPDMGSLWV EFCDEPSVGV KTMKTFVIHI QEKNFQTGIF VYQNNITPSA 

       130        140        150        160        170        180 
MKLVPSIPPA TIETFNEAAL VVNITHHELV PKHIRLSSDE KRELLKRYRL KESQLPRIQR 

       190        200        210 
ADPVALYLGL KRGEVVKIIR KSETSGRYAS YRICM 

« Hide

References

« Hide '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]"Sequence of a 4.8 kb fragment of Saccharomyces cerevisiae chromosome II including three essential open reading frames."
Baur A., Schaaff-Gerstenschlaeger I., Boles E., Miosga T., Rose M., Zimmermann F.K.
Yeast 9:289-293(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [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]"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.
[6]"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.
[7]"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.
[8]"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.
[9]"Crystal structure of RPB5, a universal eukaryotic RNA polymerase subunit and transcription factor interaction target."
Todone F., Weinzierl R.O.J., Brick P., Onesti S.
Proc. Natl. Acad. Sci. U.S.A. 97:6306-6310(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[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]"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.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX.
[21]"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.
[22]"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.
[23]"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.
[24]"Functional architecture of RNA polymerase I."
Kuhn C.D., Geiger S.R., Baumli S., Gartmann M., Gerber J., Jennebach S., Mielke T., Tschochner H., Beckmann R., Cramer P.
Cell 131:1260-1272(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (12.00 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, SUBUNIT.
[25]"Crystal structure of the 14-subunit RNA polymerase I."
Fernandez-Tornero C., Moreno-Morcillo M., Rashid U.J., Taylor N.M., Ruiz F.M., Gruene T., Legrand P., Steuerwald U., Muller C.W.
Nature 502:644-649(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, SUBUNIT.
[26]"RNA polymerase I structure and transcription regulation."
Engel C., Sainsbury S., Cheung A.C., Kostrewa D., Cramer P.
Nature 502:650-655(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53287 Genomic DNA. Translation: CAA37381.1.
X71329 Genomic DNA. Translation: CAA50472.1.
S59774 Genomic DNA. Translation: AAC60556.1.
Z36023 Genomic DNA. Translation: CAA85113.1.
BK006936 Genomic DNA. Translation: DAA07269.1.
PIRA34588.
RefSeqNP_009712.1. NM_001178502.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DZFX-ray1.90A1-215[»]
1I3QX-ray3.10E1-215[»]
1I50X-ray2.80E1-215[»]
1I6HX-ray3.30E1-215[»]
1K83X-ray2.80E1-215[»]
1NIKX-ray4.10E1-215[»]
1NT9X-ray4.20E1-215[»]
1PQVX-ray3.80E1-215[»]
1R5UX-ray4.50E1-215[»]
1R9SX-ray4.25E1-215[»]
1R9TX-ray3.50E1-215[»]
1SFOX-ray3.61E1-215[»]
1TWAX-ray3.20E1-215[»]
1TWCX-ray3.00E1-215[»]
1TWFX-ray2.30E1-215[»]
1TWGX-ray3.30E1-215[»]
1TWHX-ray3.40E1-215[»]
1WCMX-ray3.80E1-215[»]
1Y1VX-ray3.80E1-215[»]
1Y1WX-ray4.00E1-215[»]
1Y1YX-ray4.00E1-215[»]
1Y77X-ray4.50E1-215[»]
2B63X-ray3.80E1-215[»]
2B8KX-ray4.15E1-215[»]
2E2HX-ray3.95E1-215[»]
2E2IX-ray3.41E1-215[»]
2E2JX-ray3.50E1-215[»]
2JA5X-ray3.80E1-215[»]
2JA6X-ray4.00E1-215[»]
2JA7X-ray3.80E/Q1-215[»]
2JA8X-ray3.80E1-215[»]
2NVQX-ray2.90E1-215[»]
2NVTX-ray3.36E1-215[»]
2NVXX-ray3.60E1-215[»]
2NVYX-ray3.40E1-215[»]
2NVZX-ray4.30E1-215[»]
2R7ZX-ray3.80E1-215[»]
2R92X-ray3.80E1-215[»]
2R93X-ray4.00E1-215[»]
2VUMX-ray3.40E1-215[»]
2YU9X-ray3.40E1-215[»]
3CQZX-ray2.80E1-215[»]
3FKIX-ray3.88E1-215[»]
3GTGX-ray3.78E1-215[»]
3GTJX-ray3.42E1-215[»]
3GTKX-ray3.80E1-215[»]
3GTLX-ray3.38E1-215[»]
3GTMX-ray3.80E1-215[»]
3GTOX-ray4.00E1-215[»]
3GTPX-ray3.90E1-215[»]
3GTQX-ray3.80E1-215[»]
3H3VX-ray4.00F1-215[»]
3HOUX-ray3.20E/Q1-215[»]
3HOVX-ray3.50E1-215[»]
3HOWX-ray3.60E1-215[»]
3HOXX-ray3.65E1-215[»]
3HOYX-ray3.40E1-215[»]
3HOZX-ray3.65E1-215[»]
3I4MX-ray3.70E1-215[»]
3I4NX-ray3.90E1-215[»]
3J0Kelectron microscopy36.00E1-215[»]
3J1Nelectron microscopy16.00E1-215[»]
3K1FX-ray4.30E1-215[»]
3K7AX-ray3.80E1-215[»]
3M3YX-ray3.18E1-215[»]
3M4OX-ray3.57E1-215[»]
3PO2X-ray3.30E1-215[»]
3PO3X-ray3.30E1-215[»]
3QT1X-ray4.30E1-215[»]
3RZDX-ray3.30E1-215[»]
3RZOX-ray3.00E1-215[»]
3S14X-ray2.85E1-215[»]
3S15X-ray3.30E1-215[»]
3S16X-ray3.24E1-215[»]
3S17X-ray3.20E1-215[»]
3S1MX-ray3.13E1-215[»]
3S1NX-ray3.10E1-215[»]
3S1QX-ray3.30E1-215[»]
3S1RX-ray3.20E1-215[»]
3S2DX-ray3.20E1-215[»]
3S2HX-ray3.30E1-215[»]
4A3BX-ray3.50E1-215[»]
4A3CX-ray3.50E1-215[»]
4A3DX-ray3.40E1-215[»]
4A3EX-ray3.40E1-215[»]
4A3FX-ray3.50E1-215[»]
4A3GX-ray3.50E1-215[»]
4A3IX-ray3.80E1-215[»]
4A3JX-ray3.70E1-215[»]
4A3KX-ray3.50E1-215[»]
4A3LX-ray3.50E1-215[»]
4A3MX-ray3.90E1-215[»]
4A93X-ray3.40E1-215[»]
4BBRX-ray3.40E1-215[»]
4BBSX-ray3.60E1-215[»]
4BXXX-ray3.28E1-215[»]
4BXZX-ray4.80E1-215[»]
4BY1X-ray3.60E1-215[»]
4BY7X-ray3.15E1-215[»]
4C2MX-ray2.80E/T1-215[»]
4C3HX-ray3.27E1-215[»]
4C3IX-ray3.0E1-215[»]
4C3JX-ray3.35E1-215[»]
ProteinModelPortalP20434.
SMRP20434. Positions 1-215.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32853. 89 interactions.
DIPDIP-71N.
IntActP20434. 49 interactions.
MINTMINT-530046.
STRING4932.YBR154C.

Proteomic databases

MaxQBP20434.
PaxDbP20434.
PeptideAtlasP20434.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR154C; YBR154C; YBR154C.
GeneID852451.
KEGGsce:YBR154C.

Organism-specific databases

CYGDYBR154c.
SGDS000000358. RPB5.

Phylogenomic databases

eggNOGCOG2012.
GeneTreeENSGT00390000013841.
HOGENOMHOG000205213.
KOK03013.
OMADEAETYK.
OrthoDBEOG7XPZJ6.

Enzyme and pathway databases

BioCycYEAST:G3O-29104-MONOMER.

Gene expression databases

GenevestigatorP20434.

Family and domain databases

Gene3D3.40.1340.10. 1 hit.
3.90.940.20. 1 hit.
HAMAPMF_00025. RNApol_RpoH_RPB5.
InterProIPR014381. DNA_RNA_pol_RPB5_euk/virus.
IPR005571. RNA_pol_Rpb5_N.
IPR000783. RNA_pol_subH/Rpb5_C.
IPR020608. RNA_pol_subH/Rpb5_CS.
IPR020609. RpoH/RPB5.
[Graphical view]
PfamPF01191. RNA_pol_Rpb5_C. 1 hit.
PF03871. RNA_pol_Rpb5_N. 1 hit.
[Graphical view]
PIRSFPIRSF000747. RPB5. 1 hit.
ProDomPD005155. RNA_pol_subH/Rpb5_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF53036. SSF53036. 1 hit.
SSF55287. SSF55287. 1 hit.
PROSITEPS01110. RNA_POL_H_23KD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20434.
NextBio971369.
PROP20434.

Entry information

Entry nameRPAB1_YEAST
AccessionPrimary (citable) accession number: P20434
Secondary accession number(s): D6VQE9, Q02121
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 9, 2014
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: 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