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Protein

DNA-directed RNA polymerase II subunit RPB7

Gene

RPB7

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. RPB7 is part of a subcomplex with RPB4 that binds to a pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7 in the closed conformation thus preventing double-stranded DNA to enter the active site cleft. The RPB4-RPB7 subcomplex binds single-stranded DNA and RNA. The RPB4-RPB7 subcomplex recruits FCP1 to Pol II.3 Publications

GO - Molecular functioni

  • DNA-directed RNA polymerase activity Source: UniProtKB-KW
  • single-stranded DNA binding Source: SGD
  • single-stranded RNA binding Source: SGD
  • translation initiation factor binding Source: SGD

GO - Biological processi

  • nuclear-transcribed mRNA catabolic process, exonucleolytic Source: SGD
  • positive regulation of nuclear-transcribed mRNA poly(A) tail shortening Source: SGD
  • positive regulation of translational initiation Source: SGD
  • transcription, RNA-templated Source: GOC
  • transcription from RNA polymerase II promoter Source: SGD
  • transcription initiation from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Biological processi

Transcription

Enzyme and pathway databases

BioCyciYEAST:G3O-29948-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 RPB7
Short name:
RNA polymerase II subunit B7
Alternative name(s):
B16
Gene namesi
Name:RPB7
Ordered Locus Names:YDR404C
ORF Names:D9509.22
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDR404c.
EuPathDBiFungiDB:YDR404C.
SGDiS000002812. RPB7.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytoplasmic mRNA processing body Source: SGD
  • DNA-directed RNA polymerase II, core complex Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi108 – 1136Missing : Lowers nucleic-acid binding of RPB4-RPB7 by 10-fold; no effect on association with Pol II core complex; abolishes transcriptional activity of Pol II. 1 Publication
Mutagenesisi151 – 1588Missing : No effect on nucleic-acid binding of RPB4-RPB7 and on association with Pol II core complex; abolishes transcriptional activity of Pol II. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 171171DNA-directed RNA polymerase II subunit RPB7PRO_0000073993Add
BLAST

Proteomic databases

MaxQBiP34087.
PaxDbiP34087.
PeptideAtlasiP34087.

Interactioni

Subunit structurei

Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits. RPB4 and RPB7 form a subcomplex that protrudes from the 10-subunit Pol II core complex. The RPB4-RPB7 subcomplex probably associates with TFG1. Interacts with NRD1 and PAT1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RPB4P204334EBI-15790,EBI-15777

Protein-protein interaction databases

BioGridi32464. 77 interactions.
DIPiDIP-725N.
IntActiP34087. 23 interactions.
MINTiMINT-539630.

Structurei

Secondary structure

1
171
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 109Combined sources
Helixi15 – 173Combined sources
Beta strandi19 – 213Combined sources
Helixi22 – 3413Combined sources
Beta strandi37 – 393Combined sources
Turni40 – 423Combined sources
Beta strandi43 – 486Combined sources
Helixi51 – 533Combined sources
Beta strandi59 – 613Combined sources
Beta strandi63 – 653Combined sources
Beta strandi71 – 799Combined sources
Beta strandi86 – 9510Combined sources
Beta strandi98 – 1036Combined sources
Beta strandi106 – 1116Combined sources
Helixi112 – 1143Combined sources
Beta strandi117 – 1226Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi129 – 1313Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi142 – 15312Combined sources
Beta strandi156 – 1627Combined sources
Beta strandi165 – 1673Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NT9X-ray4.20G1-171[»]
1PQVX-ray3.80G1-171[»]
1WCMX-ray3.80G1-171[»]
1Y14X-ray2.30B/D1-171[»]
1Y1VX-ray3.80G1-171[»]
1Y1WX-ray4.00G1-171[»]
1Y1YX-ray4.00G1-171[»]
1Y77X-ray4.50G1-171[»]
2B63X-ray3.80G1-171[»]
2B8KX-ray4.15G1-171[»]
2JA5X-ray3.80G1-171[»]
2JA6X-ray4.00G1-171[»]
2JA7X-ray3.80G/S1-171[»]
2JA8X-ray3.80G1-171[»]
2R7ZX-ray3.80G1-171[»]
2R92X-ray3.80G1-171[»]
2R93X-ray4.00G1-171[»]
2VUMX-ray3.40G1-171[»]
3FKIX-ray3.88G1-171[»]
3H3VX-ray4.00H1-171[»]
3HOUX-ray3.20G/S1-171[»]
3HOVX-ray3.50G1-171[»]
3HOWX-ray3.60G1-171[»]
3HOXX-ray3.65G1-171[»]
3HOYX-ray3.40G1-171[»]
3HOZX-ray3.65G1-171[»]
3I4MX-ray3.70G1-171[»]
3I4NX-ray3.90G1-171[»]
3J0Kelectron microscopy36.00G1-171[»]
3J1Nelectron microscopy16.00G1-171[»]
3K1FX-ray4.30G1-171[»]
3PO2X-ray3.30G1-171[»]
3PO3X-ray3.30G1-171[»]
3QT1X-ray4.30G1-171[»]
4A3BX-ray3.50G1-171[»]
4A3CX-ray3.50G1-171[»]
4A3DX-ray3.40G1-171[»]
4A3EX-ray3.40G1-171[»]
4A3FX-ray3.50G1-171[»]
4A3GX-ray3.50G1-171[»]
4A3IX-ray3.80G1-171[»]
4A3JX-ray3.70G1-171[»]
4A3KX-ray3.50G1-171[»]
4A3LX-ray3.50G1-171[»]
4A3MX-ray3.90G1-171[»]
4A93X-ray3.40G1-171[»]
4BBRX-ray3.40G1-171[»]
4BBSX-ray3.60G1-171[»]
4BXXX-ray3.28G1-171[»]
4BXZX-ray4.80G1-171[»]
4BY1X-ray3.60G1-171[»]
4BY7X-ray3.15G1-171[»]
4V1Nelectron microscopy7.80G1-171[»]
4V1Oelectron microscopy9.70G1-171[»]
ProteinModelPortaliP34087.
SMRiP34087. Positions 1-171.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP34087.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1095.
GeneTreeiENSGT00390000008975.
HOGENOMiHOG000158201.
InParanoidiP34087.
KOiK03015.
OMAiPPQFTNN.
OrthoDBiEOG7X0VTZ.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.30.1490.120. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
IPR005576. RNA_pol_Rpb7_N.
IPR022967. S1_dom.
[Graphical view]
PfamiPF00575. S1. 1 hit.
PF03876. SHS2_Rpb7-N. 1 hit.
[Graphical view]
SMARTiSM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF88798. SSF88798. 1 hit.

Sequencei

Sequence statusi: Complete.

P34087-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFFIKDLSLN ITLHPSFFGP RMKQYLKTKL LEEVEGSCTG KFGYILCVLD
60 70 80 90 100
YDNIDIQRGR ILPTDGSAEF NVKYRAVVFK PFKGEVVDGT VVSCSQHGFE
110 120 130 140 150
VQVGPMKVFV TKHLMPQDLT FNAGSNPPSY QSSEDVITIK SRIRVKIEGC
160 170
ISQVSSIHAI GSIKEDYLGA I
Length:171
Mass (Da):19,058
Last modified:February 1, 1994 - v1
Checksum:i44C85603A93CDE67
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S59775 Genomic DNA. Translation: AAC60558.1.
U32274 Genomic DNA. Translation: AAB64844.1.
BK006938 Genomic DNA. Translation: DAA12246.1.
PIRiS30140.
RefSeqiNP_010692.3. NM_001180712.3.

Genome annotation databases

EnsemblFungiiYDR404C; YDR404C; YDR404C.
GeneIDi852013.
KEGGisce:YDR404C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S59775 Genomic DNA. Translation: AAC60558.1.
U32274 Genomic DNA. Translation: AAB64844.1.
BK006938 Genomic DNA. Translation: DAA12246.1.
PIRiS30140.
RefSeqiNP_010692.3. NM_001180712.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NT9X-ray4.20G1-171[»]
1PQVX-ray3.80G1-171[»]
1WCMX-ray3.80G1-171[»]
1Y14X-ray2.30B/D1-171[»]
1Y1VX-ray3.80G1-171[»]
1Y1WX-ray4.00G1-171[»]
1Y1YX-ray4.00G1-171[»]
1Y77X-ray4.50G1-171[»]
2B63X-ray3.80G1-171[»]
2B8KX-ray4.15G1-171[»]
2JA5X-ray3.80G1-171[»]
2JA6X-ray4.00G1-171[»]
2JA7X-ray3.80G/S1-171[»]
2JA8X-ray3.80G1-171[»]
2R7ZX-ray3.80G1-171[»]
2R92X-ray3.80G1-171[»]
2R93X-ray4.00G1-171[»]
2VUMX-ray3.40G1-171[»]
3FKIX-ray3.88G1-171[»]
3H3VX-ray4.00H1-171[»]
3HOUX-ray3.20G/S1-171[»]
3HOVX-ray3.50G1-171[»]
3HOWX-ray3.60G1-171[»]
3HOXX-ray3.65G1-171[»]
3HOYX-ray3.40G1-171[»]
3HOZX-ray3.65G1-171[»]
3I4MX-ray3.70G1-171[»]
3I4NX-ray3.90G1-171[»]
3J0Kelectron microscopy36.00G1-171[»]
3J1Nelectron microscopy16.00G1-171[»]
3K1FX-ray4.30G1-171[»]
3PO2X-ray3.30G1-171[»]
3PO3X-ray3.30G1-171[»]
3QT1X-ray4.30G1-171[»]
4A3BX-ray3.50G1-171[»]
4A3CX-ray3.50G1-171[»]
4A3DX-ray3.40G1-171[»]
4A3EX-ray3.40G1-171[»]
4A3FX-ray3.50G1-171[»]
4A3GX-ray3.50G1-171[»]
4A3IX-ray3.80G1-171[»]
4A3JX-ray3.70G1-171[»]
4A3KX-ray3.50G1-171[»]
4A3LX-ray3.50G1-171[»]
4A3MX-ray3.90G1-171[»]
4A93X-ray3.40G1-171[»]
4BBRX-ray3.40G1-171[»]
4BBSX-ray3.60G1-171[»]
4BXXX-ray3.28G1-171[»]
4BXZX-ray4.80G1-171[»]
4BY1X-ray3.60G1-171[»]
4BY7X-ray3.15G1-171[»]
4V1Nelectron microscopy7.80G1-171[»]
4V1Oelectron microscopy9.70G1-171[»]
ProteinModelPortaliP34087.
SMRiP34087. Positions 1-171.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32464. 77 interactions.
DIPiDIP-725N.
IntActiP34087. 23 interactions.
MINTiMINT-539630.

Proteomic databases

MaxQBiP34087.
PaxDbiP34087.
PeptideAtlasiP34087.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR404C; YDR404C; YDR404C.
GeneIDi852013.
KEGGisce:YDR404C.

Organism-specific databases

CYGDiYDR404c.
EuPathDBiFungiDB:YDR404C.
SGDiS000002812. RPB7.

Phylogenomic databases

eggNOGiCOG1095.
GeneTreeiENSGT00390000008975.
HOGENOMiHOG000158201.
InParanoidiP34087.
KOiK03015.
OMAiPPQFTNN.
OrthoDBiEOG7X0VTZ.

Enzyme and pathway databases

BioCyciYEAST:G3O-29948-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

EvolutionaryTraceiP34087.
NextBioi970216.
PROiP34087.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.30.1490.120. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
IPR005576. RNA_pol_Rpb7_N.
IPR022967. S1_dom.
[Graphical view]
PfamiPF00575. S1. 1 hit.
PF03876. SHS2_Rpb7-N. 1 hit.
[Graphical view]
SMARTiSM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF88798. SSF88798. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "RPB7, one of two dissociable subunits of yeast RNA polymerase II, is essential for cell viability."
    McKune K., Richards K.L., Edwards A.M., Young R.A., Woychik N.A.
    Yeast 9:295-299(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(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: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "Dissociable Rpb4-Rpb7 subassembly of RNA polymerase II binds to single-strand nucleic acid and mediates a post-recruitment step in transcription initiation."
    Orlicky S.M., Tran P.T., Sayre M.H., Edwards A.M.
    J. Biol. Chem. 276:10097-10102(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE RPB4-RPB7 COMPLEX, RNA-BINDING, MUTAGENESIS OF 108-VAL--HIS-113 AND 151-ILE--HIS-158.
  6. "Structure and mechanism of RNA polymerase II CTD phosphatases."
    Kamenski T., Heilmeier S., Meinhart A., Cramer P.
    Mol. Cell 15:399-407(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE RPB4-RPB7 COMPLEX.
  7. "Nucleocytoplasmic shuttling of the Rpb4p and Rpb7p subunits of Saccharomyces cerevisiae RNA polymerase II by two pathways."
    Selitrennik M., Duek L., Lotan R., Choder M.
    Eukaryot. Cell 5:2092-2103(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Rpb7 subunit of RNA polymerase II interacts with an RNA-binding protein involved in processing of transcripts."
    Mitsuzawa H., Kanda E., Ishihama A.
    Nucleic Acids Res. 31:4696-4701(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NRD1.
  9. "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, INTERACTION WITH TFG1.
  10. "The Rpb7p subunit of yeast RNA polymerase II plays roles in the two major cytoplasmic mRNA decay mechanisms."
    Lotan R., Goler-Baron V., Duek L., Haimovich G., Choder M.
    J. Cell Biol. 178:1133-1143(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PAT1.
  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 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) OF THE RNA POL II COMPLEX.
  14. "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.
  15. "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.
  16. "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 nameiRPB7_YEAST
AccessioniPrimary (citable) accession number: P34087
Secondary accession number(s): D6VT36
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 22, 2015
This is version 147 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 6420 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.