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Reviewed, UniProtKB/Swiss-Prot P22138 (RPA2_YEAST)

Last modified November 3, 2009. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    DNA-directed RNA polymerase I subunit RPA2
    EC=2.7.7.6
Alternative name(s):
    DNA-directed RNA polymerase I polypeptide 2
      Short name=RNA polymerase I subunit 2
    DNA-directed RNA polymerase I 135 kDa polypeptide
      Short name=A135
Gene names
Name: RPA2
Synonyms: RPA135, RRN2, SRP3
Ordered Locus Names: YPR010C
ORF Names: YP9531.03C
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1203 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol I is composed of mobile elements and RPA2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft By similarity.

Catalytic activity

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

Subunit structure

Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits.

Subcellular location

Nucleusnucleolus. Ref.9 Ref.10

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. Ref.11

Sequence similarities

Belongs to the RNA polymerase beta chain family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RPA1P109641EBI-15736,EBI-15730
RPB5P204341EBI-15736,EBI-15781

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12031203DNA-directed RNA polymerase I subunit RPA2
PRO_0000048080

Regions

Zinc finger1104 – 113128C4-type Potential

Amino acid modifications

Modified residue811Phosphoserine Ref.4 Ref.5
Modified residue881Phosphoserine Ref.4
Modified residue10851Phosphoserine Ref.5
Modified residue11161Phosphoserine Ref.5

Experimental info

Mutagenesis11041C → A: No effect; when associated with A-1107; A-1128 and A-1131. Ref.9
Mutagenesis11071C → A: Lethal. Abolishes recruitment of RPA1 to Pol I. No effect; when associated with A-1104; A-1128 and A-1131. Ref.9
Mutagenesis11271C → R: Responsible of suppression of RPA190-5 and RPA190-1 mutations.
Mutagenesis11281C → A: No effect; when associated with A-1104; A-1107 and A-1131. Ref.9
Mutagenesis11311C → A: No effect; when associated with A-1104; A-1107 and A-1128. Ref.9

Sequences

Sequence LengthMass (Da)Tools
P22138-1 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 72FA95B66F98C5F8

FASTA1,203135,742
        10         20         30         40         50         60 
MSKVIKPPGQ ARTADFRTLE RESRFINPPK DKSAFPLLQE AVQPHIGSFN ALTEGPDGGL 

        70         80         90        100        110        120 
LNLGVKDIGE KVIFDGKPLN SEDEISNSGY LGNKLSVSVE QVSIAKPMSN DGVSSAVERK 

       130        140        150        160        170        180 
VYPSESRQRL TSYRGKLLLK LKWSVNNGEE NLFEVRDCGG LPVMLQSNRC HLNKMSPYEL 

       190        200        210        220        230        240 
VQHKEESDEI GGYFIVNGIE KLIRMLIVQR RNHPMAIIRP SFANRGASYS HYGIQIRSVR 

       250        260        270        280        290        300 
PDQTSQTNVL HYLNDGQVTF RFSWRKNEYL VPVVMILKAL CHTSDREIFD GIIGNDVKDS 

       310        320        330        340        350        360 
FLTDRLELLL RGFKKRYPHL QNRTQVLQYL GDKFRVVFQA SPDQSDLEVG QEVLDRIVLV 

       370        380        390        400        410        420 
HLGKDGSQDK FRMLLFMIRK LYSLVAGECS PDNPDATQHQ EVLLGGFLYG MILKEKIDEY 

       430        440        450        460        470        480 
LQNIIAQVRM DINRGMAINF KDKRYMSRVL MRVNENIGSK MQYFLSTGNL VSQSGLDLQQ 

       490        500        510        520        530        540 
VSGYTVVAEK INFYRFISHF RMVHRGSFFA QLKTTTVRKL LPESWGFLCP VHTPDGSPCG 

       550        560        570        580        590        600 
LLNHFAHKCR ISTQQSDVSR IPSILYSLGV APASHTFAAG PSLCCVQIDG KIIGWVSHEQ 

       610        620        630        640        650        660 
GKIIADTLRY WKVEGKTPGL PIDLEIGYVP PSTRGQYPGL YLFGGHSRML RPVRYLPLDK 

       670        680        690        700        710        720 
EDIVGPFEQV YMNIAVTPQE IQNNVHTHVE FTPTNILSIL ANLTPFSDFN QSPRNMYQCQ 

       730        740        750        760        770        780 
MGKQTMGTPG VALCHRSDNK LYRLQTGQTP IVKANLYDDY GMDNFPNGFN AVVAVISYTG 

       790        800        810        820        830        840 
YDMDDAMIIN KSADERGFGY GTMYKTEKVD LALNRNRGDP ITQHFGFGND EWPKEWLEKL 

       850        860        870        880        890        900 
DEDGLPYIGT YVEEGDPICA YFDDTLNKTK IKTYHSSEPA YIEEVNLIGD ESNKFQELQT 

       910        920        930        940        950        960 
VSIKYRIRRT PQIGDKFSSR HGQKGVCSRK WPTIDMPFSE TGIQPDIIIN PHAFPSRMTI 

       970        980        990       1000       1010       1020 
GMFVESLAGK AGALHGIAQD STPWIFNEDD TPADYFGEQL AKAGYNYHGN EPMYSGATGE 

      1030       1040       1050       1060       1070       1080 
ELRADIYVGV VYYQRLRHMV NDKFQVRSTG PVNSLTMQPV KGRKRHGGIR VGEMERDALI 

      1090       1100       1110       1120       1130       1140 
GHGTSFLLQD RLLNSSDYTQ ASVCRECGSI LTTQQSVPRI GSISTVCCRR CSMRFEDAKK 

      1150       1160       1170       1180       1190       1200 
LLTKSEDGEK IFIDDSQIWE DGQGNKFVGG NETTTVAIPF VLKYLDSELS AMGIRLRYNV 


EPK 

« Hide

References

« Hide 'large scale' references
[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: 1990281] [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. 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: 9169875] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]"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: 11717393] [Abstract]
Cited for: IDENTIFICATION IN THE RNA POL I COMPLEX.
[4]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81 AND SER-88, MASS SPECTROMETRY.
[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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; SER-1085 AND SER-1116, MASS SPECTROMETRY.
[6]"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: 12145213] [Abstract]
Cited for: ELECTRON MICROSCOPY OF THE RNA POLYMERASE I COMPLEX.
[7]"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: 11918799] [Abstract]
Cited for: IDENTIFICATION IN THE RNA POL I COMPLEX.
[8]"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: 12407181] [Abstract]
Cited for: IDENTIFICATION IN THE RNA POL I COMPLEX.
[9]"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: 14555487] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-1104; CYS-1107; CYS-1128 AND CYS-1131.
[10]"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: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[11]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

U31900 Genomic DNA. Translation: AAA97589.1.
M62804 Genomic DNA. Translation: AAA34993.1.
Z49919 Genomic DNA. Translation: CAA90154.1.
Z71255 Genomic DNA. Translation: CAA95050.1.
PIRA39607.
RefSeqNP_015335.1.

3D structure databases

HSSPHSSP built from PDB template 1I50 based on UniProtKB P08518.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:135N.
IntActP22138. 59 interactions.
STRINGP22138.

Proteomic databases

PeptideAtlasP22138.
PRIDEP22138.

Genome annotation databases

EnsemblYPR010C; YPR010C; YPR010C; Saccharomyces cerevisiae. [Genome view]
GeneID856119.
GenomeReviewsGene locus YPR010C in contig U00094_GR.
KEGGsce:YPR010C.
NMPDRfig|4932.3.peg.6469.

Organism-specific databases

CYGDYPR010c.
SGDS000006214. RPA135.

Phylogenomic databases

HOGENOMP22138.
OMAPATHEEI.

Enzyme and pathway databases

BRENDA2.7.7.6. 250.

Gene expression databases

ArrayExpressP22138.
GenevestigatorP22138.
GermOnlineYPR010C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR015712. DNA-dir_RNA_pol_su2.
IPR007120. DNA-dir_RNA_pol_su2_6.
IPR007121. RNA_pol_bsu_CS.
IPR007644. RNA_pol_bsu_protrusion.
IPR009674. RNA_pol_Rpa2-specific.
IPR007642. RNA_pol_Rpb2_2.
IPR007645. RNA_pol_Rpb2_3.
IPR007647. RNA_pol_Rpb2_5.
IPR007641. RNA_pol_Rpb2_7.
[Graphical view]
PANTHERPTHR20856. RNA_pol_I_sub2. 1 hit.
PfamPF06883. 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.
PF04567. RNA_pol_Rpb2_5. 1 hit.
PF00562. RNA_pol_Rpb2_6. 1 hit.
PF04560. RNA_pol_Rpb2_7. 1 hit.
[Graphical view]
PROSITEPS01166. RNA_POL_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio981198.

Entry information

Entry nameRPA2_YEAST
AccessionPrimary (citable) accession number: P22138
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: November 3, 2009
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents