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Protein

DNA-directed RNA polymerase I subunit RPA135

Gene

RPA135

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 polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. Besides, RNA polymerase I has intrinsic RNA cleavage activity. RPA190 and RPA135 both contribute to the polymerase catalytic activity and together form the Pol I active center. In addition, subunit RPA12 contributes a catalytic zinc ribbon that is required for RNA cleavage by Pol I. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA190 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition.3 Publications

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1104 – 113128C4-typeAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW
  • ribonucleoside binding Source: InterPro
  • RNA polymerase I activity Source: UniProtKB

GO - Biological processi

  • ribosome biogenesis Source: UniProtKB-KW
  • transcription from RNA polymerase I promoter Source: UniProtKB
  • transcription of nuclear large rRNA transcript from RNA polymerase I promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Ribosome biogenesis, Transcription

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-34172-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase I subunit RPA135 (EC:2.7.7.6)
Alternative name(s):
DNA-directed RNA polymerase I 135 kDa polypeptide
Short name:
A135
DNA-directed RNA polymerase I polypeptide 2
Short name:
RNA polymerase I subunit 2
Gene namesi
Name:RPA135
Synonyms:RPA2, RRN2, SRP3
Ordered Locus Names:YPR010C
ORF Names:YP9531.03C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR010C.
SGDiS000006214. RPA135.

Subcellular locationi

GO - Cellular componenti

  • DNA-directed RNA polymerase I complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1104 – 11041C → A: No effect; when associated with A-1107; A-1128 and A-1131. 1 Publication
Mutagenesisi1107 – 11071C → A: Lethal. Abolishes recruitment of RPA1 to Pol I. No effect; when associated with A-1104; A-1128 and A-1131. 1 Publication
Mutagenesisi1127 – 11271C → R: Responsible of suppression of RPA190-5 and RPA190-1 mutations.
Mutagenesisi1128 – 11281C → A: No effect; when associated with A-1104; A-1107 and A-1131. 1 Publication
Mutagenesisi1131 – 11311C → A: No effect; when associated with A-1104; A-1107 and A-1128. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 12031202DNA-directed RNA polymerase I subunit RPA135PRO_0000048080Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei81 – 811PhosphoserineCombined sources
Modified residuei1156 – 11561PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP22138.
PeptideAtlasiP22138.

PTM databases

iPTMnetiP22138.

Interactioni

Subunit structurei

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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RPA190P109644EBI-15736,EBI-15730

Protein-protein interaction databases

BioGridi36188. 140 interactions.
DIPiDIP-135N.
IntActiP22138. 51 interactions.
MINTiMINT-423299.

Structurei

Secondary structure

1
1203
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 269Combined sources
Beta strandi30 – 323Combined sources
Helixi36 – 5015Combined sources
Turni51 – 533Combined sources
Helixi56 – 583Combined sources
Helixi60 – 689Combined sources
Beta strandi71 – 744Combined sources
Helixi86 – 894Combined sources
Beta strandi94 – 10411Combined sources
Beta strandi108 – 1114Combined sources
Beta strandi117 – 1204Combined sources
Helixi123 – 1297Combined sources
Beta strandi134 – 14512Combined sources
Turni146 – 1494Combined sources
Beta strandi150 – 16213Combined sources
Turni171 – 1744Combined sources
Helixi177 – 1826Combined sources
Beta strandi194 – 1963Combined sources
Beta strandi199 – 2035Combined sources
Beta strandi205 – 2095Combined sources
Beta strandi214 – 2185Combined sources
Helixi220 – 2256Combined sources
Beta strandi229 – 23911Combined sources
Beta strandi245 – 2539Combined sources
Beta strandi258 – 2647Combined sources
Beta strandi267 – 2726Combined sources
Helixi273 – 2808Combined sources
Helixi285 – 2939Combined sources
Helixi300 – 31314Combined sources
Turni314 – 3163Combined sources
Helixi323 – 33412Combined sources
Turni335 – 3395Combined sources
Beta strandi342 – 3443Combined sources
Helixi346 – 35712Combined sources
Helixi360 – 3623Combined sources
Helixi367 – 38519Combined sources
Beta strandi387 – 3893Combined sources
Helixi397 – 3993Combined sources
Beta strandi400 – 4034Combined sources
Helixi405 – 43430Combined sources
Helixi443 – 4519Combined sources
Helixi457 – 46711Combined sources
Beta strandi485 – 4873Combined sources
Helixi493 – 4997Combined sources
Beta strandi502 – 5043Combined sources
Helixi507 – 5104Combined sources
Turni516 – 5183Combined sources
Helixi522 – 5243Combined sources
Turni525 – 5273Combined sources
Turni537 – 5415Combined sources
Beta strandi542 – 5454Combined sources
Turni558 – 5603Combined sources
Helixi561 – 5677Combined sources
Helixi573 – 5753Combined sources
Beta strandi583 – 5886Combined sources
Beta strandi591 – 5966Combined sources
Helixi598 – 61417Combined sources
Beta strandi618 – 6203Combined sources
Beta strandi625 – 6295Combined sources
Beta strandi633 – 6364Combined sources
Beta strandi639 – 6435Combined sources
Beta strandi649 – 6557Combined sources
Turni656 – 6594Combined sources
Beta strandi660 – 6645Combined sources
Helixi666 – 6694Combined sources
Beta strandi674 – 6774Combined sources
Helixi678 – 6803Combined sources
Turni683 – 6853Combined sources
Beta strandi687 – 6893Combined sources
Helixi693 – 6964Combined sources
Helixi699 – 7035Combined sources
Helixi707 – 7093Combined sources
Helixi712 – 72211Combined sources
Helixi733 – 7353Combined sources
Beta strandi739 – 7457Combined sources
Beta strandi751 – 7533Combined sources
Helixi755 – 7595Combined sources
Helixi762 – 7643Combined sources
Beta strandi769 – 7779Combined sources
Beta strandi779 – 7813Combined sources
Beta strandi786 – 7905Combined sources
Helixi791 – 7955Combined sources
Turni796 – 7994Combined sources
Beta strandi801 – 81010Combined sources
Beta strandi813 – 8153Combined sources
Beta strandi823 – 8264Combined sources
Helixi835 – 8384Combined sources
Beta strandi844 – 8463Combined sources
Beta strandi857 – 8637Combined sources
Turni864 – 8674Combined sources
Beta strandi868 – 8736Combined sources
Beta strandi880 – 8889Combined sources
Beta strandi892 – 8943Combined sources
Beta strandi900 – 90910Combined sources
Beta strandi916 – 9194Combined sources
Beta strandi924 – 9318Combined sources
Turni933 – 9353Combined sources
Beta strandi938 – 9425Combined sources
Beta strandi946 – 9494Combined sources
Helixi951 – 9533Combined sources
Turni955 – 9573Combined sources
Helixi960 – 97516Combined sources
Beta strandi988 – 9903Combined sources
Helixi992 – 100312Combined sources
Beta strandi1009 – 10113Combined sources
Turni1016 – 10183Combined sources
Beta strandi1026 – 103611Combined sources
Helixi1040 – 10434Combined sources
Beta strandi1045 – 10495Combined sources
Turni1054 – 10563Combined sources
Helixi1063 – 10653Combined sources
Beta strandi1069 – 10713Combined sources
Helixi1073 – 108210Combined sources
Helixi1085 – 10928Combined sources
Turni1093 – 10975Combined sources
Beta strandi1098 – 11047Combined sources
Turni1105 – 11073Combined sources
Beta strandi1110 – 11156Combined sources
Beta strandi1120 – 11223Combined sources
Beta strandi1126 – 11316Combined sources
Helixi1135 – 11395Combined sources
Helixi1155 – 11573Combined sources
Beta strandi1158 – 11603Combined sources
Beta strandi1166 – 11683Combined sources
Beta strandi1173 – 11797Combined sources
Helixi1180 – 119112Combined sources
Beta strandi1194 – 12018Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C2MX-ray2.80B/Q1-1203[»]
4C3HX-ray3.27B1-1203[»]
4C3IX-ray3.0B1-1203[»]
4C3JX-ray3.35B1-1203[»]
4YM7X-ray5.50AB/BB/CB/DB/EB/FB1-1203[»]
ProteinModelPortaliP22138.
SMRiP22138. Positions 898-1097.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RNA polymerase beta chain family.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1104 – 113128C4-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00760000119399.
HOGENOMiHOG000222963.
InParanoidiP22138.
KOiK03002.
OMAiHTVRYDA.
OrthoDBiEOG7PVWXQ.

Family and domain databases

Gene3Di2.40.270.10. 2 hits.
2.40.50.150. 1 hit.
3.90.1110.10. 1 hit.
InterProiIPR015712. DNA-dir_RNA_pol_su2.
IPR007120. DNA-dir_RNA_pol_su2_6.
IPR007121. RNA_pol_bsu_CS.
IPR007644. RNA_pol_bsu_protrusion.
IPR007642. RNA_pol_Rpb2_2.
IPR007645. RNA_pol_Rpb2_3.
IPR007641. RNA_pol_Rpb2_7.
IPR014724. RNA_pol_RPB2_OB-fold.
IPR009674. Rpa2_dom_4.
[Graphical view]
PANTHERiPTHR20856. PTHR20856. 2 hits.
PfamiPF06883. RNA_pol_Rpa2_4. 1 hit.
PF04563. RNA_pol_Rpb2_1. 1 hit.
PF04561. RNA_pol_Rpb2_2. 1 hit.
PF04565. RNA_pol_Rpb2_3. 1 hit.
PF00562. RNA_pol_Rpb2_6. 1 hit.
PF04560. RNA_pol_Rpb2_7. 1 hit.
[Graphical view]
PROSITEiPS01166. RNA_POL_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22138-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKVIKPPGQ ARTADFRTLE RESRFINPPK DKSAFPLLQE AVQPHIGSFN
60 70 80 90 100
ALTEGPDGGL LNLGVKDIGE KVIFDGKPLN SEDEISNSGY LGNKLSVSVE
110 120 130 140 150
QVSIAKPMSN DGVSSAVERK VYPSESRQRL TSYRGKLLLK LKWSVNNGEE
160 170 180 190 200
NLFEVRDCGG LPVMLQSNRC HLNKMSPYEL VQHKEESDEI GGYFIVNGIE
210 220 230 240 250
KLIRMLIVQR RNHPMAIIRP SFANRGASYS HYGIQIRSVR PDQTSQTNVL
260 270 280 290 300
HYLNDGQVTF RFSWRKNEYL VPVVMILKAL CHTSDREIFD GIIGNDVKDS
310 320 330 340 350
FLTDRLELLL RGFKKRYPHL QNRTQVLQYL GDKFRVVFQA SPDQSDLEVG
360 370 380 390 400
QEVLDRIVLV HLGKDGSQDK FRMLLFMIRK LYSLVAGECS PDNPDATQHQ
410 420 430 440 450
EVLLGGFLYG MILKEKIDEY LQNIIAQVRM DINRGMAINF KDKRYMSRVL
460 470 480 490 500
MRVNENIGSK MQYFLSTGNL VSQSGLDLQQ VSGYTVVAEK INFYRFISHF
510 520 530 540 550
RMVHRGSFFA QLKTTTVRKL LPESWGFLCP VHTPDGSPCG LLNHFAHKCR
560 570 580 590 600
ISTQQSDVSR IPSILYSLGV APASHTFAAG PSLCCVQIDG KIIGWVSHEQ
610 620 630 640 650
GKIIADTLRY WKVEGKTPGL PIDLEIGYVP PSTRGQYPGL YLFGGHSRML
660 670 680 690 700
RPVRYLPLDK EDIVGPFEQV YMNIAVTPQE IQNNVHTHVE FTPTNILSIL
710 720 730 740 750
ANLTPFSDFN QSPRNMYQCQ MGKQTMGTPG VALCHRSDNK LYRLQTGQTP
760 770 780 790 800
IVKANLYDDY GMDNFPNGFN AVVAVISYTG YDMDDAMIIN KSADERGFGY
810 820 830 840 850
GTMYKTEKVD LALNRNRGDP ITQHFGFGND EWPKEWLEKL DEDGLPYIGT
860 870 880 890 900
YVEEGDPICA YFDDTLNKTK IKTYHSSEPA YIEEVNLIGD ESNKFQELQT
910 920 930 940 950
VSIKYRIRRT PQIGDKFSSR HGQKGVCSRK WPTIDMPFSE TGIQPDIIIN
960 970 980 990 1000
PHAFPSRMTI GMFVESLAGK AGALHGIAQD STPWIFNEDD TPADYFGEQL
1010 1020 1030 1040 1050
AKAGYNYHGN EPMYSGATGE ELRADIYVGV VYYQRLRHMV NDKFQVRSTG
1060 1070 1080 1090 1100
PVNSLTMQPV KGRKRHGGIR VGEMERDALI GHGTSFLLQD RLLNSSDYTQ
1110 1120 1130 1140 1150
ASVCRECGSI LTTQQSVPRI GSISTVCCRR CSMRFEDAKK LLTKSEDGEK
1160 1170 1180 1190 1200
IFIDDSQIWE DGQGNKFVGG NETTTVAIPF VLKYLDSELS AMGIRLRYNV

EPK
Length:1,203
Mass (Da):135,742
Last modified:August 1, 1991 - v1
Checksum:i72FA95B66F98C5F8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31900 Genomic DNA. Translation: AAA97589.1.
M62804 Genomic DNA. Translation: AAA34993.1.
Z49919 Genomic DNA. Translation: CAA90154.1.
Z71255 Genomic DNA. Translation: CAA95050.1.
BK006949 Genomic DNA. Translation: DAA11437.1.
PIRiA39607.
RefSeqiNP_015335.1. NM_001184107.1.

Genome annotation databases

EnsemblFungiiYPR010C; YPR010C; YPR010C.
GeneIDi856119.
KEGGisce:YPR010C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31900 Genomic DNA. Translation: AAA97589.1.
M62804 Genomic DNA. Translation: AAA34993.1.
Z49919 Genomic DNA. Translation: CAA90154.1.
Z71255 Genomic DNA. Translation: CAA95050.1.
BK006949 Genomic DNA. Translation: DAA11437.1.
PIRiA39607.
RefSeqiNP_015335.1. NM_001184107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C2MX-ray2.80B/Q1-1203[»]
4C3HX-ray3.27B1-1203[»]
4C3IX-ray3.0B1-1203[»]
4C3JX-ray3.35B1-1203[»]
4YM7X-ray5.50AB/BB/CB/DB/EB/FB1-1203[»]
ProteinModelPortaliP22138.
SMRiP22138. Positions 898-1097.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36188. 140 interactions.
DIPiDIP-135N.
IntActiP22138. 51 interactions.
MINTiMINT-423299.

PTM databases

iPTMnetiP22138.

Proteomic databases

MaxQBiP22138.
PeptideAtlasiP22138.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR010C; YPR010C; YPR010C.
GeneIDi856119.
KEGGisce:YPR010C.

Organism-specific databases

EuPathDBiFungiDB:YPR010C.
SGDiS000006214. RPA135.

Phylogenomic databases

GeneTreeiENSGT00760000119399.
HOGENOMiHOG000222963.
InParanoidiP22138.
KOiK03002.
OMAiHTVRYDA.
OrthoDBiEOG7PVWXQ.

Enzyme and pathway databases

BioCyciYEAST:G3O-34172-MONOMER.

Miscellaneous databases

PROiP22138.

Family and domain databases

Gene3Di2.40.270.10. 2 hits.
2.40.50.150. 1 hit.
3.90.1110.10. 1 hit.
InterProiIPR015712. DNA-dir_RNA_pol_su2.
IPR007120. DNA-dir_RNA_pol_su2_6.
IPR007121. RNA_pol_bsu_CS.
IPR007644. RNA_pol_bsu_protrusion.
IPR007642. RNA_pol_Rpb2_2.
IPR007645. RNA_pol_Rpb2_3.
IPR007641. RNA_pol_Rpb2_7.
IPR014724. RNA_pol_RPB2_OB-fold.
IPR009674. Rpa2_dom_4.
[Graphical view]
PANTHERiPTHR20856. PTHR20856. 2 hits.
PfamiPF06883. RNA_pol_Rpa2_4. 1 hit.
PF04563. RNA_pol_Rpb2_1. 1 hit.
PF04561. RNA_pol_Rpb2_2. 1 hit.
PF04565. RNA_pol_Rpb2_3. 1 hit.
PF00562. RNA_pol_Rpb2_6. 1 hit.
PF04560. RNA_pol_Rpb2_7. 1 hit.
[Graphical view]
PROSITEiPS01166. RNA_POL_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Suppressor analysis of temperature-sensitive mutations of the largest subunit of RNA polymerase I in Saccharomyces cerevisiae: a suppressor gene encodes the second-largest subunit of RNA polymerase I."
    Yano R., Nomura M.
    Mol. Cell. Biol. 11:754-764(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 971-989 AND 1003-1020.
  2. "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.
    , 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.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "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.
  5. "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-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81 AND SER-1156, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Localization of the yeast RNA polymerase I-specific subunits."
    Bischler N., Brino L., Carles C., Riva M., Tschochner H., Mallouh V., Schultz P.
    EMBO J. 21:4136-4144(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ELECTRON MICROSCOPY OF THE RNA POLYMERASE I COMPLEX.
  9. "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.
  10. "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.
  11. "Role of second-largest RNA polymerase I subunit Zn-binding domain in enzyme assembly."
    Naryshkina T., Bruning A., Gadal O., Severinov K.
    Eukaryot. Cell 2:1046-1052(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-1104; CYS-1107; CYS-1128 AND CYS-1131.
  12. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  14. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (12.00 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE POL I COMPLEX IN COMPLEX WITH ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, ZINC-BINDING, SUBUNIT.
  16. "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, CATALYTIC ACTIVITY, ZINC-BINDING, SUBUNIT.

Entry informationi

Entry nameiRPA2_YEAST
AccessioniPrimary (citable) accession number: P22138
Secondary accession number(s): D6W421
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: June 8, 2016
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Three distinct zinc-containing RNA polymerases are found in eukaryotic nuclei: polymerase I for the ribosomal RNA precursor, polymerase II for the mRNA precursor, and polymerase III for 5S and tRNA genes.
Present with 14100 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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

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 one 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.