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P20435 (RPAB2_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 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length155 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 polymerases are composed of mobile elements that move relative to each other. In Pol II, RPB6 is part of the clamp element and together with parts of RPB1 and RPB2 forms a pocket to which the RPB4-RPB7 subcomplex binds. Ref.26 Ref.27 Ref.28

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.5 Ref.6 Ref.7 Ref.26 Ref.27 Ref.28

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 processRibosome biogenesis
Transcription
   Cellular componentCytoplasm
DNA-directed RNA polymerase
Nucleus
   PTMPhosphoprotein
   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.27. Source: UniProtKB

transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 12697831. Source: SGD

transcription from RNA polymerase III promoter

Inferred from mutant phenotype PubMed 12697831. 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.27. 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

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

RNA polymerase I activity

Inferred from direct assay Ref.27. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11805826PubMed 16429126PubMed 18467557. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RPA190P109643EBI-15786,EBI-15730

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 155155DNA-directed RNA polymerases I, II, and III subunit RPABC2 HAMAP-Rule MF_00192
PRO_0000133797

Regions

Region111 – 13222Leucine-zipper HAMAP-Rule MF_00192

Amino acid modifications

Modified residue241Phosphoserine Ref.11

Secondary structure

................ 155
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20435 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: AA3DEF529F94A5E4

FASTA15517,910
        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 

« 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]"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. expand/collapse author list , 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 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]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
[26]"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.
[27]"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.
[28]"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
X53288 Genomic DNA. Translation: CAA37382.1.
M33924 Genomic DNA. Translation: AAA34989.1.
U25841 Genomic DNA. Translation: AAB64616.1.
BK006949 Genomic DNA. Translation: DAA11603.1.
PIRRNBYR6. S13307.
RefSeqNP_015513.1. NM_001184284.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I3QX-ray3.10F1-155[»]
1I50X-ray2.80F1-155[»]
1I6HX-ray3.30F1-155[»]
1K83X-ray2.80F1-155[»]
1NIKX-ray4.10F1-155[»]
1NT9X-ray4.20F1-155[»]
1PQVX-ray3.80F1-155[»]
1R5UX-ray4.50F1-155[»]
1R9SX-ray4.25F1-155[»]
1R9TX-ray3.50F1-155[»]
1SFOX-ray3.61F1-155[»]
1TWAX-ray3.20F1-155[»]
1TWCX-ray3.00F1-155[»]
1TWFX-ray2.30F1-155[»]
1TWGX-ray3.30F1-155[»]
1TWHX-ray3.40F1-155[»]
1WCMX-ray3.80F1-155[»]
1Y1VX-ray3.80F1-155[»]
1Y1WX-ray4.00F1-155[»]
1Y1YX-ray4.00F1-155[»]
1Y77X-ray4.50F1-155[»]
2B63X-ray3.80F1-155[»]
2B8KX-ray4.15F1-155[»]
2E2HX-ray3.95F1-155[»]
2E2IX-ray3.41F1-155[»]
2E2JX-ray3.50F1-155[»]
2JA5X-ray3.80F1-155[»]
2JA6X-ray4.00F1-155[»]
2JA7X-ray3.80F/R1-155[»]
2JA8X-ray3.80F1-155[»]
2NVQX-ray2.90F1-155[»]
2NVTX-ray3.36F1-155[»]
2NVXX-ray3.60F1-155[»]
2NVYX-ray3.40F1-155[»]
2NVZX-ray4.30F1-155[»]
2R7ZX-ray3.80F1-155[»]
2R92X-ray3.80F1-155[»]
2R93X-ray4.00F1-155[»]
2VUMX-ray3.40F1-155[»]
2YU9X-ray3.40F1-155[»]
3CQZX-ray2.80F1-155[»]
3FKIX-ray3.88F1-155[»]
3GTGX-ray3.78F1-155[»]
3GTJX-ray3.42F1-155[»]
3GTKX-ray3.80F1-155[»]
3GTLX-ray3.38F1-155[»]
3GTMX-ray3.80F1-155[»]
3GTOX-ray4.00F1-155[»]
3GTPX-ray3.90F1-155[»]
3GTQX-ray3.80F1-155[»]
3H3VX-ray4.00G1-155[»]
3HOUX-ray3.20F/R1-155[»]
3HOVX-ray3.50F1-155[»]
3HOWX-ray3.60F1-155[»]
3HOXX-ray3.65F1-155[»]
3HOYX-ray3.40F1-155[»]
3HOZX-ray3.65F1-155[»]
3I4MX-ray3.70F1-155[»]
3I4NX-ray3.90F1-155[»]
3J0Kelectron microscopy36.00F72-155[»]
3J1Nelectron microscopy16.00F72-155[»]
3K1FX-ray4.30F1-155[»]
3K7AX-ray3.80F1-155[»]
3M3YX-ray3.18F1-155[»]
3M4OX-ray3.57F1-155[»]
3PO2X-ray3.30F1-155[»]
3PO3X-ray3.30F1-155[»]
3QT1X-ray4.30F1-155[»]
3RZDX-ray3.30F1-155[»]
3RZOX-ray3.00F1-155[»]
3S14X-ray2.85F1-155[»]
3S15X-ray3.30F1-155[»]
3S16X-ray3.24F1-155[»]
3S17X-ray3.20F1-155[»]
3S1MX-ray3.13F1-155[»]
3S1NX-ray3.10F1-155[»]
3S1QX-ray3.30F1-155[»]
3S1RX-ray3.20F1-155[»]
3S2DX-ray3.20F1-155[»]
3S2HX-ray3.30F1-155[»]
4A3BX-ray3.50F1-155[»]
4A3CX-ray3.50F1-155[»]
4A3DX-ray3.40F1-155[»]
4A3EX-ray3.40F1-155[»]
4A3FX-ray3.50F1-155[»]
4A3GX-ray3.50F1-155[»]
4A3IX-ray3.80F1-155[»]
4A3JX-ray3.70F1-155[»]
4A3KX-ray3.50F1-155[»]
4A3LX-ray3.50F1-155[»]
4A3MX-ray3.90F1-155[»]
4A93X-ray3.40F1-155[»]
4BBRX-ray3.40F1-155[»]
4BBSX-ray3.60F1-155[»]
4BXXX-ray3.28F1-155[»]
4BXZX-ray4.80F1-155[»]
4BY1X-ray3.60F1-155[»]
4BY7X-ray3.15F1-155[»]
4C2MX-ray2.80F/U1-155[»]
4C3HX-ray3.27F1-155[»]
4C3IX-ray3.0F1-155[»]
4C3JX-ray3.35F1-155[»]
ProteinModelPortalP20435.
SMRP20435. Positions 55-154.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36359. 97 interactions.
DIPDIP-2194N.
IntActP20435. 38 interactions.
MINTMINT-569579.
STRING4932.YPR187W.

Proteomic databases

MaxQBP20435.
PaxDbP20435.
PeptideAtlasP20435.
PRIDEP20435.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPR187W; YPR187W; YPR187W.
GeneID856317.
KEGGsce:YPR187W.

Organism-specific databases

CYGDYPR187w.
SGDS000006391. RPO26.

Phylogenomic databases

eggNOGCOG1758.
GeneTreeENSGT00390000010415.
HOGENOMHOG000225272.
KOK03014.
OMAINGGFGP.
OrthoDBEOG7MWH92.

Enzyme and pathway databases

BioCycYEAST:G3O-34310-MONOMER.

Gene expression databases

GenevestigatorP20435.

Family and domain databases

Gene3D3.90.940.10. 1 hit.
HAMAPMF_00192. RNApol_arch_K.
InterProIPR020708. DNA-dir_RNA_polK_14-18kDa_CS.
IPR006110. Pol_omega/K/RPB6.
IPR012293. RNAP_RPB6_omega.
IPR028363. RPB6.
IPR006111. RpoK/Rpb6.
[Graphical view]
PANTHERPTHR10773. PTHR10773. 1 hit.
PfamPF01192. RNA_pol_Rpb6. 1 hit.
[Graphical view]
PIRSFPIRSF500154. RPB6. 1 hit.
PIRSF000778. RpoK/RPB6. 1 hit.
SUPFAMSSF63562. SSF63562. 1 hit.
PROSITEPS01111. RNA_POL_K_14KD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20435.
NextBio981703.
PROP20435.

Entry information

Entry nameRPAB2_YEAST
AccessionPrimary (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: 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 XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: 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