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P20436 (RPAB3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. 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 RPABC3

Short name=RNA polymerases I, II, and III subunit ABC3
Alternative name(s):
ABC14.4
ABC14.5
DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide
Gene names
Name:RPB8
Ordered Locus Names:YOR224C
ORF Names:YOR50-14
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length146 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Ref.27 Ref.28 Ref.29

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. Directly interacts with POLR2A. Ref.7 Ref.27 Ref.28 Ref.29

Subcellular location

Nucleus Ref.8.

Miscellaneous

Present with 6210 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the eukaryotic RPB8 RNA polymerase subunit family.

Ontologies

Keywords
   Biological processRibosome biogenesis
Transcription
   Cellular componentDNA-directed RNA polymerase
Nucleus
   LigandDNA-binding
   PTMAcetylation
Phosphoprotein
   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.28. Source: UniProtKB

transcription from RNA polymerase II promoter

Inferred from physical interaction PubMed 11486042. Source: SGD

transcription from RNA polymerase III promoter

Inferred from genetic interaction PubMed 9927738. 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.28. 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.28. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16606443PubMed 20489023. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RSP5P399403EBI-15794,EBI-16219

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 146145DNA-directed RNA polymerases I, II, and III subunit RPABC3
PRO_0000074001

Regions

Region16 – 3924Non-specific ssDNA binding By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.11
Modified residue681Phosphothreonine Ref.10

Secondary structure

.......................... 146
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20436 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 5B71693FE6FD8863

FASTA14616,511
        10         20         30         40         50         60 
MSNTLFDDIF QVSEVDPGRY NKVCRIEAAS TTQDQCKLTL DINVELFPVA AQDSLTVTIA 

        70         80         90        100        110        120 
SSLNLEDTPA NDSSATRSWR PPQAGDRSLA DDYDYVMYGT AYKFEEVSKD LIAVYYSFGG 

       130        140 
LLMRLEGNYR NLNNLKQENA YLLIRR 

« 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 and analysis of a 33 kb fragment from the right arm of chromosome XV of the yeast Saccharomyces cerevisiae."
Galisson F., Dujon B.
Yeast 12:877-885(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[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]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"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.
[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.
[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]"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 THR-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[12]"Eukaryotic RNA polymerase subunit RPB8 is a new relative of the OB family."
Krapp S., Kelly G., Reischi J., Weinzierl R.O.J., Matthews S.
Nat. Struct. Biol. 5:110-114(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"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).
[22]"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.
[23]"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.
[24]"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.
[25]"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.
[26]"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.
[27]"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.
[28]"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.
[29]"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
X53289 Genomic DNA. Translation: CAA37383.1.
X92441 Genomic DNA. Translation: CAA63187.1.
Z75132 Genomic DNA. Translation: CAA99443.1.
AY693087 Genomic DNA. Translation: AAT93106.1.
BK006948 Genomic DNA. Translation: DAA10995.1.
PIRC34588.
RefSeqNP_014867.1. NM_001183643.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A1DNMR-A1-146[»]
1I3QX-ray3.10H1-146[»]
1I50X-ray2.80H1-146[»]
1I6HX-ray3.30H1-146[»]
1K83X-ray2.80H1-146[»]
1NIKX-ray4.10H1-146[»]
1NT9X-ray4.20H1-146[»]
1PQVX-ray3.80H1-146[»]
1R5UX-ray4.50H1-146[»]
1R9SX-ray4.25H1-146[»]
1R9TX-ray3.50H1-146[»]
1SFOX-ray3.61H1-146[»]
1TWAX-ray3.20H1-146[»]
1TWCX-ray3.00H1-146[»]
1TWFX-ray2.30H1-146[»]
1TWGX-ray3.30H1-146[»]
1TWHX-ray3.40H1-146[»]
1WCMX-ray3.80H1-146[»]
1Y1VX-ray3.80H1-146[»]
1Y1WX-ray4.00H1-146[»]
1Y1YX-ray4.00H1-146[»]
1Y77X-ray4.50H1-146[»]
2B63X-ray3.80H1-146[»]
2B8KX-ray4.15H1-146[»]
2E2HX-ray3.95H1-146[»]
2E2IX-ray3.41H1-146[»]
2E2JX-ray3.50H1-146[»]
2JA5X-ray3.80H1-146[»]
2JA6X-ray4.00H1-146[»]
2JA7X-ray3.80H/T1-146[»]
2JA8X-ray3.80H1-146[»]
2NVQX-ray2.90H1-146[»]
2NVTX-ray3.36H1-146[»]
2NVXX-ray3.60H1-146[»]
2NVYX-ray3.40H1-146[»]
2NVZX-ray4.30H1-146[»]
2R7ZX-ray3.80H1-146[»]
2R92X-ray3.80H1-146[»]
2R93X-ray4.00H1-146[»]
2VUMX-ray3.40H1-146[»]
2YU9X-ray3.40H1-146[»]
3CQZX-ray2.80H1-146[»]
3FKIX-ray3.88H1-146[»]
3GTGX-ray3.78H1-146[»]
3GTJX-ray3.42H1-146[»]
3GTKX-ray3.80H1-146[»]
3GTLX-ray3.38H1-146[»]
3GTMX-ray3.80H1-146[»]
3GTOX-ray4.00H1-146[»]
3GTPX-ray3.90H1-146[»]
3GTQX-ray3.80H1-146[»]
3H3VX-ray4.00I1-146[»]
3HOUX-ray3.20H/T1-146[»]
3HOVX-ray3.50H1-146[»]
3HOWX-ray3.60H1-146[»]
3HOXX-ray3.65H1-146[»]
3HOYX-ray3.40H1-146[»]
3HOZX-ray3.65H1-146[»]
3I4MX-ray3.70H1-146[»]
3I4NX-ray3.90H1-146[»]
3J0Kelectron microscopy36.00H1-146[»]
3J1Nelectron microscopy16.00H1-146[»]
3K1FX-ray4.30H1-146[»]
3K7AX-ray3.80H1-146[»]
3M3YX-ray3.18H1-146[»]
3M4OX-ray3.57H1-146[»]
3PO2X-ray3.30H1-146[»]
3PO3X-ray3.30H1-146[»]
3QT1X-ray4.30H1-146[»]
3RZDX-ray3.30H1-146[»]
3RZOX-ray3.00H1-146[»]
3S14X-ray2.85H1-146[»]
3S15X-ray3.30H1-146[»]
3S16X-ray3.24H1-146[»]
3S17X-ray3.20H1-146[»]
3S1MX-ray3.13H1-146[»]
3S1NX-ray3.10H1-146[»]
3S1QX-ray3.30H1-146[»]
3S1RX-ray3.20H1-146[»]
3S2DX-ray3.20H1-146[»]
3S2HX-ray3.30H1-146[»]
4A3BX-ray3.50H1-146[»]
4A3CX-ray3.50H1-146[»]
4A3DX-ray3.40H1-146[»]
4A3EX-ray3.40H1-146[»]
4A3FX-ray3.50H1-146[»]
4A3GX-ray3.50H1-146[»]
4A3IX-ray3.80H1-146[»]
4A3JX-ray3.70H1-146[»]
4A3KX-ray3.50H1-146[»]
4A3LX-ray3.50H1-146[»]
4A3MX-ray3.90H1-146[»]
4A93X-ray3.40H1-146[»]
4BBRX-ray3.40H1-146[»]
4BBSX-ray3.60H1-146[»]
4BXXX-ray3.28H1-146[»]
4BXZX-ray4.80H1-146[»]
4BY1X-ray3.60H1-146[»]
4BY7X-ray3.15H1-146[»]
4C2MX-ray2.80H/W1-146[»]
4C3HX-ray3.27H1-146[»]
4C3IX-ray3.0H1-146[»]
4C3JX-ray3.35H1-146[»]
ProteinModelPortalP20436.
SMRP20436. Positions 1-146.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34618. 72 interactions.
DIPDIP-2195N.
IntActP20436. 20 interactions.
MINTMINT-507506.
STRING4932.YOR224C.

Proteomic databases

MaxQBP20436.
PaxDbP20436.
PeptideAtlasP20436.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR224C; YOR224C; YOR224C.
GeneID854399.
KEGGsce:YOR224C.

Organism-specific databases

CYGDYOR224c.
SGDS000005750. RPB8.

Phylogenomic databases

eggNOGNOG279425.
GeneTreeENSGT00390000018195.
HOGENOMHOG000175572.
KOK03016.
OMAWRPDGKG.
OrthoDBEOG78D7XD.

Enzyme and pathway databases

BioCycYEAST:G3O-33723-MONOMER.

Gene expression databases

GenevestigatorP20436.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
InterProIPR012340. NA-bd_OB-fold.
IPR005570. RNA_pol_Rpb8.
[Graphical view]
PANTHERPTHR10917. PTHR10917. 1 hit.
PfamPF03870. RNA_pol_Rpb8. 1 hit.
[Graphical view]
PIRSFPIRSF000779. RNA_pol_Rpb8. 1 hit.
SMARTSM00658. RPOL8c. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP20436.
NextBio976571.
PROP20436.

Entry information

Entry nameRPAB3_YEAST
AccessionPrimary (citable) accession number: P20436
Secondary accession number(s): D6W2S9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 9, 2014
This is version 148 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 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