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UniProtKB/Swiss-Prot entry P22138


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RPA2_YEAST
Primary accession number P22138
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1991
Sequence was last modified on August 1, 1991 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 82)
Name and origin of the protein
Protein name DNA-directed RNA polymerase I subunit RPA2
Synonyms EC 2.7.7.6
DNA-directed RNA polymerase I polypeptide 2
RNA polymerase I subunit 2
DNA-directed RNA polymerase I 135 kDa polypeptide
A135
Gene name
Name: RPA2
Synonyms: RPA135, RRN2, SRP3
OrderedLocusNames: YPR010C
ORFNames: YP9531.03C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 971-989 AND 1003-1020.
PubMed=1990281 [NCBI, ExPASy, EBI, Israel, Japan]
Yano R., Nomura M.;
"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.";
Mol. Cell. Biol. 11:754-764(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169875 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[3]
IDENTIFICATION IN THE RNA POL I COMPLEX.
DOI=10.1073/pnas.231181398; PubMed=11717393 [NCBI, ExPASy, EBI, Israel, Japan]
Fath S., Milkereit P., Peyroche G., Riva M., Carles C., Tschochner H.;
"Differential roles of phosphorylation in the formation of transcriptional active RNA polymerase I.";
Proc. Natl. Acad. Sci. U.S.A. 98:14334-14339(2001).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81 AND SER-88, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; SER-1085 AND SER-1116, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[6]
ELECTRON MICROSCOPY OF THE RNA POLYMERASE I COMPLEX.
DOI=10.1093/emboj/cdf392; PubMed=12145213 [NCBI, ExPASy, EBI, Israel, Japan]
Bischler N., Brino L., Carles C., Riva M., Tschochner H., Mallouh V., Schultz P.;
"Localization of the yeast RNA polymerase I-specific subunits.";
EMBO J. 21:4136-4144(2002).
[7]
IDENTIFICATION IN THE RNA POL I COMPLEX.
PubMed=11918799 [NCBI, ExPASy, EBI, Israel, Japan]
Van Mullem V., Landrieux E., Vandenhaute J., Thuriaux P.;
"Rpa12p, a conserved RNA polymerase I subunit with two functional domains.";
Mol. Microbiol. 43:1105-1113(2002).
[8]
IDENTIFICATION IN THE RNA POL I COMPLEX.
DOI=10.1073/pnas.232580799; PubMed=12407181 [NCBI, ExPASy, EBI, Israel, Japan]
Peyroche G., Levillain E., Siaut M., Callebaut I., Schultz P., Sentenac A., Riva M., Carles C.;
"The A14-A43 heterodimer subunit in yeast RNA pol I and their relationship to Rpb4-Rpb7 pol II subunits.";
Proc. Natl. Acad. Sci. U.S.A. 99:14670-14675(2002).
[9]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-1104; CYS-1107; CYS-1128 AND CYS-1131.
DOI=10.1128/EC.2.5.1046-1052.2003; PubMed=14555487 [NCBI, ExPASy, EBI, Israel, Japan]
Naryshkina T., Bruning A., Gadal O., Severinov K.;
"Role of second-largest RNA polymerase I subunit Zn-binding domain in enzyme assembly.";
Eukaryot. Cell 2:1046-1052(2003).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[11]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
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: Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits.
  • SUBCELLULAR LOCATION: Nucleus, nucleolus.
  • 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.
  • MISCELLANEOUS: Present with 14100 molecules/cell in log phase SD medium.
  • SIMILARITY: Belongs to the RNA polymerase beta chain family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U31900; AAA97589.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M62804; AAA34993.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z49919; CAA90154.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z71255; CAA95050.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A39607; A39607.
RefSeq NP_015335.1; -.
3D structure databases
HSSP P08518; 1I50. [HSSP ENTRY / PDB]
ModBase P22138.
Protein-protein interaction databases
DIP DIP:135N; -.
Organism-specific databases
CYGD YPR010c; -.
SGD S000006214; RPA135.
Yeast-GFP YPR010C.
Gene expression databases
ArrayExpress P22138; -.
GermOnline YPR010C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005736; Cellular component: DNA-directed RNA polymerase I complex (traceable author statement from SGD).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from InterPro).
GO:0003899; Molecular function: DNA-directed RNA polymerase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006350; Biological process: transcription (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR015712; 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 of domain structure.
PANTHER PTHR20856; RNA_pol_I_sub2; 1.
Pfam PF06883; RNA_pol_Rpa2_4; 1.
PF04563; RNA_pol_Rpb2_1; 1.
PF04561; RNA_pol_Rpb2_2; 1.
PF04565; RNA_pol_Rpb2_3; 1.
PF04567; RNA_pol_Rpb2_5; 1.
PF00562; RNA_pol_Rpb2_6; 1.
PF04560; RNA_pol_Rpb2_7; 1.
Pfam graphical view of domain structure.
PROSITE PS01166; RNA_POL_BETA; 1.
ProtoNet P22138.
Proteomic databases
PeptideAtlas P22138; -.
Genome annotation databases
Ensembl YPR010C; Saccharomyces cerevisiae. [Contig view]
GeneID 856119; -.
GenomeReviews U00094_GR; YPR010C.
KEGG sce:YPR010C; -.
NMPDR fig|4932.3.peg.6469; -.
Phylogenomic databases
HOGENOM P22138; -.
Other
LinkHub P22138; -.
NextBio 981198; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein; Transcription; Transferase; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1203  1203     DNA-directed RNA polymerase I subunit RPA2. PRO_0000048080
ZN_FING   1104   1131  28     C4-type (Potential). 
MOD_RES   81     81        Phosphoserine. 
MOD_RES   88     88        Phosphoserine. 
MOD_RES   1085   1085        Phosphoserine. 
MOD_RES   1116   1116        Phosphoserine. 
MUTAGEN   1104   1104        C->A: No effect; when associated with A-1107; A-1128 and A-1131. 
MUTAGEN   1107   1107        C->A: Lethal. Abolishes recruitment of RPA1 to Pol I. No effect; when associated with A-1104; A-1128 and A-1131. 
MUTAGEN   1127   1127        C->R: Responsible of suppression of RPA190-5 and RPA190-1 mutations. 
MUTAGEN   1128   1128        C->A: No effect; when associated with A-1104; A-1107 and A-1131. 
MUTAGEN   1131   1131        C->A: No effect; when associated with A-1104; A-1107 and A-1128. 
Sequence information
Length: 1203 AA [This is the length of the unprocessed precursor] Molecular weight: 135742 Da [This is the MW of the unprocessed precursor] CRC64: 72FA95B66F98C5F8 [This is a checksum on the sequence]
        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 

P22138 in FASTA format

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