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Protein

DNA-directed RNA polymerase II subunit RPB11

Gene

RPB11

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB11 is part of the core element with the central large cleft. Seems to be involved transcript termination.1 Publication

GO - Molecular functioni

GO - Biological processi

  • termination of RNA polymerase II transcription Source: SGD
  • transcription, RNA-templated Source: GOC
  • transcription from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Biological processi

Transcription

Enzyme and pathway databases

BioCyciYEAST:G3O-33422-MONOMER.
ReactomeiREACT_273109. Formation of the Early Elongation Complex.
REACT_273984. Dual incision reaction in TC-NER.
REACT_277632. mRNA Capping.
REACT_294700. mRNA Splicing - Minor Pathway.
REACT_296055. RNA Polymerase II Promoter Escape.
REACT_300180. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_310018. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_315180. RNA Polymerase II Pre-transcription Events.
REACT_317581. Processing of Capped Intron-Containing Pre-mRNA.
REACT_322294. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_331999. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_341636. Transcription-coupled NER (TC-NER).
REACT_345860. RNA Polymerase II Transcription Initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase II subunit RPB11
Short name:
RNA polymerase II subunit B11
Alternative name(s):
B13.6
DNA-directed RNA polymerase II 13.6 kDa polypeptide
Gene namesi
Name:RPB11
Ordered Locus Names:YOL005C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XV

Organism-specific databases

CYGDiYOL005c.
EuPathDBiFungiDB:YOL005C.
SGDiS000005365. RPB11.

Subcellular locationi

GO - Cellular componenti

  • DNA-directed RNA polymerase II, core complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi108 – 1081E → G or V: Transcript termination readthrough. 1 Publication
Mutagenesisi108 – 1081E → K: Transcript termination readthrough. Lethal. 1 Publication
Mutagenesisi111 – 1111L → P: Transcript termination readthrough. 1 Publication
Mutagenesisi114 – 1141L → P: Transcript termination readthrough. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 120120DNA-directed RNA polymerase II subunit RPB11PRO_0000149315Add
BLAST

Proteomic databases

MaxQBiP38902.
PaxDbiP38902.
PeptideAtlasiP38902.

Interactioni

Subunit structurei

Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RPB3P163704EBI-15806,EBI-15773

Protein-protein interaction databases

BioGridi34399. 48 interactions.
DIPiDIP-937N.
IntActiP38902. 15 interactions.
MINTiMINT-618340.

Structurei

Secondary structure

1
120
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 93Combined sources
Beta strandi18 – 203Combined sources
Beta strandi21 – 233Combined sources
Beta strandi25 – 273Combined sources
Beta strandi30 – 378Combined sources
Helixi40 – 5011Combined sources
Beta strandi51 – 533Combined sources
Beta strandi56 – 627Combined sources
Beta strandi66 – 683Combined sources
Beta strandi70 – 778Combined sources
Helixi83 – 10826Combined sources
Turni109 – 1113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I3QX-ray3.10K1-120[»]
1I50X-ray2.80K1-120[»]
1I6HX-ray3.30K1-120[»]
1K83X-ray2.80K1-120[»]
1NIKX-ray4.10K1-120[»]
1NT9X-ray4.20K1-120[»]
1PQVX-ray3.80K1-120[»]
1R5UX-ray4.50K1-120[»]
1R9SX-ray4.25K1-120[»]
1R9TX-ray3.50K1-120[»]
1SFOX-ray3.61K1-120[»]
1TWAX-ray3.20K1-120[»]
1TWCX-ray3.00K1-120[»]
1TWFX-ray2.30K1-120[»]
1TWGX-ray3.30K1-120[»]
1TWHX-ray3.40K1-120[»]
1WCMX-ray3.80K1-120[»]
1Y1VX-ray3.80K1-120[»]
1Y1WX-ray4.00K1-120[»]
1Y1YX-ray4.00K1-120[»]
1Y77X-ray4.50K1-120[»]
2B63X-ray3.80K1-120[»]
2B8KX-ray4.15K1-120[»]
2E2HX-ray3.95K1-120[»]
2E2IX-ray3.41K1-120[»]
2E2JX-ray3.50K1-120[»]
2JA5X-ray3.80K1-120[»]
2JA6X-ray4.00K1-120[»]
2JA7X-ray3.80K/W1-120[»]
2JA8X-ray3.80K1-120[»]
2NVQX-ray2.90K1-120[»]
2NVTX-ray3.36K1-120[»]
2NVXX-ray3.60K1-120[»]
2NVYX-ray3.40K1-120[»]
2NVZX-ray4.30K1-120[»]
2R7ZX-ray3.80K1-120[»]
2R92X-ray3.80K1-120[»]
2R93X-ray4.00K1-120[»]
2VUMX-ray3.40K1-120[»]
2YU9X-ray3.40K1-120[»]
3CQZX-ray2.80K1-120[»]
3FKIX-ray3.88K1-120[»]
3GTGX-ray3.78K1-120[»]
3GTJX-ray3.42K1-120[»]
3GTKX-ray3.80K1-120[»]
3GTLX-ray3.38K1-120[»]
3GTMX-ray3.80K1-120[»]
3GTOX-ray4.00K1-120[»]
3GTPX-ray3.90K1-120[»]
3GTQX-ray3.80K1-120[»]
3H3VX-ray4.00L1-120[»]
3HOUX-ray3.20K/W1-120[»]
3HOVX-ray3.50K1-120[»]
3HOWX-ray3.60K1-120[»]
3HOXX-ray3.65K1-120[»]
3HOYX-ray3.40K1-120[»]
3HOZX-ray3.65K1-120[»]
3I4MX-ray3.70K1-120[»]
3I4NX-ray3.90K1-120[»]
3J0Kelectron microscopy36.00K1-120[»]
3J1Nelectron microscopy16.00K1-120[»]
3K1FX-ray4.30K1-120[»]
3K7AX-ray3.80K1-120[»]
3M3YX-ray3.18K1-120[»]
3M4OX-ray3.57K1-120[»]
3PO2X-ray3.30K1-120[»]
3PO3X-ray3.30K1-120[»]
3QT1X-ray4.30K1-120[»]
3RZDX-ray3.30K1-120[»]
3RZOX-ray3.00K1-120[»]
3S14X-ray2.85K1-120[»]
3S15X-ray3.30K1-120[»]
3S16X-ray3.24K1-120[»]
3S17X-ray3.20K1-120[»]
3S1MX-ray3.13K1-120[»]
3S1NX-ray3.10K1-120[»]
3S1QX-ray3.30K1-120[»]
3S1RX-ray3.20K1-120[»]
3S2DX-ray3.20K1-120[»]
3S2HX-ray3.30K1-120[»]
4A3BX-ray3.50K1-120[»]
4A3CX-ray3.50K1-120[»]
4A3DX-ray3.40K1-120[»]
4A3EX-ray3.40K1-120[»]
4A3FX-ray3.50K1-120[»]
4A3GX-ray3.50K1-120[»]
4A3IX-ray3.80K1-120[»]
4A3JX-ray3.70K1-120[»]
4A3KX-ray3.50K1-120[»]
4A3LX-ray3.50K1-120[»]
4A3MX-ray3.90K1-120[»]
4A93X-ray3.40K1-120[»]
4BBRX-ray3.40K1-120[»]
4BBSX-ray3.60K1-120[»]
4BXXX-ray3.28K1-120[»]
4BXZX-ray4.80K1-120[»]
4BY1X-ray3.60K1-120[»]
4BY7X-ray3.15K1-120[»]
4V1Melectron microscopy6.60K1-120[»]
4V1Nelectron microscopy7.80K1-120[»]
4V1Oelectron microscopy9.70K1-120[»]
4X67X-ray4.10K1-120[»]
4X6AX-ray3.96K1-120[»]
ProteinModelPortaliP38902.
SMRiP38902. Positions 1-114.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38902.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1761.
GeneTreeiENSGT00550000074975.
HOGENOMiHOG000179862.
InParanoidiP38902.
KOiK03008.
OMAiFAAYKVE.
OrthoDBiEOG7T4MZH.

Family and domain databases

InterProiIPR009025. RBP11-like_dimer.
IPR008193. RNA_pol_Rpb11_13-16kDa_CS.
[Graphical view]
SUPFAMiSSF55257. SSF55257. 1 hit.
PROSITEiPS01154. RNA_POL_L_13KD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38902-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAPDRFELF LLGEGESKLK IDPDTKAPNA VVITFEKEDH TLGNLIRAEL
60 70 80 90 100
LNDRKVLFAA YKVEHPFFAR FKLRIQTTEG YDPKDALKNA CNSIINKLGA
110 120
LKTNFETEWN LQTLAADDAF
Length:120
Mass (Da):13,616
Last modified:February 1, 1995 - v1
Checksum:iA98D109C5FF8E356
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S62624 Genomic DNA. Translation: AAB27135.1.
Z74747 Genomic DNA. Translation: CAA99004.1.
AY557998 Genomic DNA. Translation: AAS56324.1.
BK006948 Genomic DNA. Translation: DAA10778.1.
PIRiS58933.
RefSeqiNP_014638.1. NM_001183259.1.

Genome annotation databases

EnsemblFungiiYOL005C; YOL005C; YOL005C.
GeneIDi854157.
KEGGisce:YOL005C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S62624 Genomic DNA. Translation: AAB27135.1.
Z74747 Genomic DNA. Translation: CAA99004.1.
AY557998 Genomic DNA. Translation: AAS56324.1.
BK006948 Genomic DNA. Translation: DAA10778.1.
PIRiS58933.
RefSeqiNP_014638.1. NM_001183259.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I3QX-ray3.10K1-120[»]
1I50X-ray2.80K1-120[»]
1I6HX-ray3.30K1-120[»]
1K83X-ray2.80K1-120[»]
1NIKX-ray4.10K1-120[»]
1NT9X-ray4.20K1-120[»]
1PQVX-ray3.80K1-120[»]
1R5UX-ray4.50K1-120[»]
1R9SX-ray4.25K1-120[»]
1R9TX-ray3.50K1-120[»]
1SFOX-ray3.61K1-120[»]
1TWAX-ray3.20K1-120[»]
1TWCX-ray3.00K1-120[»]
1TWFX-ray2.30K1-120[»]
1TWGX-ray3.30K1-120[»]
1TWHX-ray3.40K1-120[»]
1WCMX-ray3.80K1-120[»]
1Y1VX-ray3.80K1-120[»]
1Y1WX-ray4.00K1-120[»]
1Y1YX-ray4.00K1-120[»]
1Y77X-ray4.50K1-120[»]
2B63X-ray3.80K1-120[»]
2B8KX-ray4.15K1-120[»]
2E2HX-ray3.95K1-120[»]
2E2IX-ray3.41K1-120[»]
2E2JX-ray3.50K1-120[»]
2JA5X-ray3.80K1-120[»]
2JA6X-ray4.00K1-120[»]
2JA7X-ray3.80K/W1-120[»]
2JA8X-ray3.80K1-120[»]
2NVQX-ray2.90K1-120[»]
2NVTX-ray3.36K1-120[»]
2NVXX-ray3.60K1-120[»]
2NVYX-ray3.40K1-120[»]
2NVZX-ray4.30K1-120[»]
2R7ZX-ray3.80K1-120[»]
2R92X-ray3.80K1-120[»]
2R93X-ray4.00K1-120[»]
2VUMX-ray3.40K1-120[»]
2YU9X-ray3.40K1-120[»]
3CQZX-ray2.80K1-120[»]
3FKIX-ray3.88K1-120[»]
3GTGX-ray3.78K1-120[»]
3GTJX-ray3.42K1-120[»]
3GTKX-ray3.80K1-120[»]
3GTLX-ray3.38K1-120[»]
3GTMX-ray3.80K1-120[»]
3GTOX-ray4.00K1-120[»]
3GTPX-ray3.90K1-120[»]
3GTQX-ray3.80K1-120[»]
3H3VX-ray4.00L1-120[»]
3HOUX-ray3.20K/W1-120[»]
3HOVX-ray3.50K1-120[»]
3HOWX-ray3.60K1-120[»]
3HOXX-ray3.65K1-120[»]
3HOYX-ray3.40K1-120[»]
3HOZX-ray3.65K1-120[»]
3I4MX-ray3.70K1-120[»]
3I4NX-ray3.90K1-120[»]
3J0Kelectron microscopy36.00K1-120[»]
3J1Nelectron microscopy16.00K1-120[»]
3K1FX-ray4.30K1-120[»]
3K7AX-ray3.80K1-120[»]
3M3YX-ray3.18K1-120[»]
3M4OX-ray3.57K1-120[»]
3PO2X-ray3.30K1-120[»]
3PO3X-ray3.30K1-120[»]
3QT1X-ray4.30K1-120[»]
3RZDX-ray3.30K1-120[»]
3RZOX-ray3.00K1-120[»]
3S14X-ray2.85K1-120[»]
3S15X-ray3.30K1-120[»]
3S16X-ray3.24K1-120[»]
3S17X-ray3.20K1-120[»]
3S1MX-ray3.13K1-120[»]
3S1NX-ray3.10K1-120[»]
3S1QX-ray3.30K1-120[»]
3S1RX-ray3.20K1-120[»]
3S2DX-ray3.20K1-120[»]
3S2HX-ray3.30K1-120[»]
4A3BX-ray3.50K1-120[»]
4A3CX-ray3.50K1-120[»]
4A3DX-ray3.40K1-120[»]
4A3EX-ray3.40K1-120[»]
4A3FX-ray3.50K1-120[»]
4A3GX-ray3.50K1-120[»]
4A3IX-ray3.80K1-120[»]
4A3JX-ray3.70K1-120[»]
4A3KX-ray3.50K1-120[»]
4A3LX-ray3.50K1-120[»]
4A3MX-ray3.90K1-120[»]
4A93X-ray3.40K1-120[»]
4BBRX-ray3.40K1-120[»]
4BBSX-ray3.60K1-120[»]
4BXXX-ray3.28K1-120[»]
4BXZX-ray4.80K1-120[»]
4BY1X-ray3.60K1-120[»]
4BY7X-ray3.15K1-120[»]
4V1Melectron microscopy6.60K1-120[»]
4V1Nelectron microscopy7.80K1-120[»]
4V1Oelectron microscopy9.70K1-120[»]
4X67X-ray4.10K1-120[»]
4X6AX-ray3.96K1-120[»]
ProteinModelPortaliP38902.
SMRiP38902. Positions 1-114.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34399. 48 interactions.
DIPiDIP-937N.
IntActiP38902. 15 interactions.
MINTiMINT-618340.

Proteomic databases

MaxQBiP38902.
PaxDbiP38902.
PeptideAtlasiP38902.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL005C; YOL005C; YOL005C.
GeneIDi854157.
KEGGisce:YOL005C.

Organism-specific databases

CYGDiYOL005c.
EuPathDBiFungiDB:YOL005C.
SGDiS000005365. RPB11.

Phylogenomic databases

eggNOGiCOG1761.
GeneTreeiENSGT00550000074975.
HOGENOMiHOG000179862.
InParanoidiP38902.
KOiK03008.
OMAiFAAYKVE.
OrthoDBiEOG7T4MZH.

Enzyme and pathway databases

BioCyciYEAST:G3O-33422-MONOMER.
ReactomeiREACT_273109. Formation of the Early Elongation Complex.
REACT_273984. Dual incision reaction in TC-NER.
REACT_277632. mRNA Capping.
REACT_294700. mRNA Splicing - Minor Pathway.
REACT_296055. RNA Polymerase II Promoter Escape.
REACT_300180. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_310018. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_315180. RNA Polymerase II Pre-transcription Events.
REACT_317581. Processing of Capped Intron-Containing Pre-mRNA.
REACT_322294. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_331999. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_341636. Transcription-coupled NER (TC-NER).
REACT_345860. RNA Polymerase II Transcription Initiation.

Miscellaneous databases

EvolutionaryTraceiP38902.
NextBioi975923.
PROiP38902.

Family and domain databases

InterProiIPR009025. RBP11-like_dimer.
IPR008193. RNA_pol_Rpb11_13-16kDa_CS.
[Graphical view]
SUPFAMiSSF55257. SSF55257. 1 hit.
PROSITEiPS01154. RNA_POL_L_13KD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast RNA polymerase II subunit RPB11 is related to a subunit shared by RNA polymerase I and III."
    Woychik N.A., McKune K., Lane W.S., Young R.A.
    Gene Expr. 3:77-82(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-37; 75-84; 98-102 AND 103-116.
    Strain: X2180-2.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "cis- and trans-Acting determinants of transcription termination by yeast RNA polymerase II."
    Steinmetz E.J., Ng S.B., Cloute J.P., Brow D.A.
    Mol. Cell. Biol. 26:2688-2696(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLU-108; LEU-111 AND LEU-114.
  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] [Europe PMC] [Abstract]
    Cited for: ELECTRON MICROSCOPY OF THE RNA POL II/TFIIF COMPLEX.
  8. "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.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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).
  16. "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.
  17. "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.
  18. "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.
  19. "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.

Entry informationi

Entry nameiRPB11_YEAST
AccessioniPrimary (citable) accession number: P38902
Secondary accession number(s): D6W262
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 22, 2015
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4280 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.