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Protein

DNA-directed RNA polymerase I subunit RPA190

Gene

RPA190

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi62 – 621Zinc 1Combined sources1 Publication
Metal bindingi65 – 651Zinc 1Combined sources1 Publication
Metal bindingi72 – 721Zinc 1Combined sources1 Publication
Metal bindingi75 – 751Zinc 1; via tele nitrogenCombined sources1 Publication
Metal bindingi102 – 1021Zinc 2Combined sources1 Publication
Metal bindingi105 – 1051Zinc 2Combined sources1 Publication
Metal bindingi233 – 2331Zinc 2Combined sources1 Publication
Metal bindingi236 – 2361Zinc 2Combined sources1 Publication
Metal bindingi627 – 6271Magnesium; catalyticBy similarity
Metal bindingi629 – 6291Magnesium; catalyticBy similarity
Metal bindingi631 – 6311Magnesium; catalyticBy similarity

GO - Molecular functioni

  • DNA binding Source: InterPro
  • RNA polymerase I activity Source: UniProtKB
  • zinc ion binding Source: InterPro

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

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-33816-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase I subunit RPA190 (EC:2.7.7.6)
Alternative name(s):
DNA-directed RNA polymerase I 190 kDa polypeptide
Short name:
A190
DNA-directed RNA polymerase I largest subunit
Gene namesi
Name:RPA190
Synonyms:RPA1, RRN1
Ordered Locus Names:YOR341W
ORF Names:O6276
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR341W.
SGDiS000005868. RPA190.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16641664DNA-directed RNA polymerase I subunit RPA190PRO_0000073930Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei889 – 8891PhosphoserineCombined sources
Modified residuei1636 – 16361PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP10964.
PeptideAtlasiP10964.
TopDownProteomicsiP10964.

PTM databases

iPTMnetiP10964.

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
PRP43P531312EBI-15730,EBI-505
RPA135P221384EBI-15730,EBI-15736
RPC40P077035EBI-15730,EBI-15831
RPO26P204353EBI-15730,EBI-15786

Protein-protein interaction databases

BioGridi34724. 112 interactions.
DIPiDIP-999N.
IntActiP10964. 37 interactions.
MINTiMINT-613626.

Structurei

Secondary structure

1
1664
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 189Combined sources
Helixi21 – 277Combined sources
Helixi52 – 543Combined sources
Turni63 – 653Combined sources
Turni69 – 713Combined sources
Beta strandi77 – 8610Combined sources
Helixi88 – 903Combined sources
Helixi91 – 10010Combined sources
Turni103 – 1053Combined sources
Beta strandi107 – 1104Combined sources
Helixi112 – 12615Combined sources
Helixi130 – 1356Combined sources
Helixi136 – 1383Combined sources
Helixi175 – 19824Combined sources
Turni199 – 2013Combined sources
Helixi210 – 22819Combined sources
Turni234 – 2363Combined sources
Beta strandi242 – 2454Combined sources
Beta strandi247 – 2493Combined sources
Beta strandi251 – 2544Combined sources
Helixi258 – 2669Combined sources
Turni267 – 2704Combined sources
Helixi317 – 33014Combined sources
Helixi332 – 3387Combined sources
Helixi352 – 3554Combined sources
Beta strandi356 – 3627Combined sources
Helixi365 – 3673Combined sources
Beta strandi371 – 3733Combined sources
Beta strandi376 – 3783Combined sources
Helixi381 – 40424Combined sources
Turni408 – 4103Combined sources
Helixi415 – 43824Combined sources
Helixi440 – 4423Combined sources
Helixi456 – 4616Combined sources
Beta strandi462 – 4643Combined sources
Helixi466 – 4705Combined sources
Beta strandi472 – 48615Combined sources
Beta strandi488 – 4903Combined sources
Beta strandi494 – 4974Combined sources
Helixi499 – 5024Combined sources
Beta strandi506 – 5105Combined sources
Turni513 – 5153Combined sources
Helixi516 – 52510Combined sources
Turni526 – 5283Combined sources
Beta strandi529 – 5313Combined sources
Beta strandi533 – 5375Combined sources
Beta strandi543 – 5453Combined sources
Helixi551 – 5588Combined sources
Turni559 – 5624Combined sources
Helixi568 – 5703Combined sources
Beta strandi576 – 5805Combined sources
Beta strandi586 – 5905Combined sources
Helixi597 – 5993Combined sources
Beta strandi600 – 6078Combined sources
Beta strandi613 – 6164Combined sources
Helixi618 – 6203Combined sources
Helixi621 – 6244Combined sources
Beta strandi628 – 6303Combined sources
Beta strandi632 – 6365Combined sources
Helixi641 – 6499Combined sources
Helixi653 – 6564Combined sources
Turni660 – 6623Combined sources
Helixi672 – 6809Combined sources
Beta strandi686 – 6883Combined sources
Helixi689 – 70012Combined sources
Beta strandi703 – 7053Combined sources
Beta strandi708 – 7114Combined sources
Beta strandi718 – 7236Combined sources
Beta strandi725 – 7273Combined sources
Helixi728 – 73912Combined sources
Beta strandi742 – 7443Combined sources
Beta strandi749 – 7524Combined sources
Helixi757 – 7593Combined sources
Beta strandi768 – 7725Combined sources
Beta strandi775 – 7784Combined sources
Helixi783 – 7864Combined sources
Helixi793 – 82432Combined sources
Helixi830 – 8334Combined sources
Helixi837 – 84711Combined sources
Helixi848 – 8503Combined sources
Helixi853 – 8619Combined sources
Helixi873 – 88412Combined sources
Helixi886 – 91126Combined sources
Turni912 – 9154Combined sources
Beta strandi916 – 9183Combined sources
Turni920 – 9223Combined sources
Helixi924 – 9307Combined sources
Helixi937 – 9448Combined sources
Helixi976 – 9794Combined sources
Turni986 – 9883Combined sources
Helixi992 – 101120Combined sources
Helixi1017 – 102711Combined sources
Beta strandi1036 – 10394Combined sources
Beta strandi1045 – 10495Combined sources
Helixi1050 – 10523Combined sources
Helixi1057 – 10593Combined sources
Helixi1066 – 10705Combined sources
Helixi1073 – 10808Combined sources
Helixi1082 – 10887Combined sources
Beta strandi1089 – 10924Combined sources
Helixi1093 – 110715Combined sources
Beta strandi1109 – 11113Combined sources
Helixi1113 – 11153Combined sources
Helixi1123 – 11264Combined sources
Turni1129 – 11313Combined sources
Helixi1138 – 115013Combined sources
Helixi1152 – 11554Combined sources
Beta strandi1157 – 11604Combined sources
Helixi1163 – 117513Combined sources
Helixi1185 – 119410Combined sources
Helixi1196 – 12005Combined sources
Helixi1218 – 12269Combined sources
Beta strandi1237 – 12426Combined sources
Beta strandi1244 – 12463Combined sources
Helixi1248 – 125811Combined sources
Helixi1263 – 12664Combined sources
Beta strandi1267 – 12759Combined sources
Beta strandi1288 – 12969Combined sources
Helixi1299 – 13068Combined sources
Helixi1310 – 13189Combined sources
Helixi1320 – 133516Combined sources
Beta strandi1344 – 13463Combined sources
Helixi1364 – 13663Combined sources
Helixi1369 – 137810Combined sources
Beta strandi1382 – 13843Combined sources
Helixi1389 – 13946Combined sources
Helixi1442 – 145211Combined sources
Beta strandi1454 – 14629Combined sources
Turni1464 – 14663Combined sources
Beta strandi1469 – 14768Combined sources
Helixi1485 – 14939Combined sources
Beta strandi1497 – 14993Combined sources
Beta strandi1504 – 15085Combined sources
Beta strandi1518 – 15236Combined sources
Helixi1526 – 15294Combined sources
Helixi1530 – 15323Combined sources
Turni1533 – 15353Combined sources
Helixi1538 – 15403Combined sources
Beta strandi1542 – 15443Combined sources
Helixi1546 – 15538Combined sources
Helixi1555 – 157218Combined sources
Helixi1579 – 158911Combined sources
Turni1590 – 15923Combined sources
Helixi1600 – 16034Combined sources
Helixi1609 – 16135Combined sources
Helixi1618 – 162710Combined sources
Helixi1637 – 16437Combined sources
Helixi1650 – 16523Combined sources
Beta strandi1653 – 16619Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C2MX-ray2.80A/P1-1664[»]
4C3HX-ray3.27A1-1664[»]
4C3IX-ray3.0A1-1664[»]
4C3JX-ray3.35A1-1664[»]
4YM7X-ray5.50AA/BA/CA/DA/EA/FA1-1664[»]
ProteinModelPortaliP10964.
SMRiP10964. Positions 1178-1209, 1438-1663.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni992 – 100413Bridging helixBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the RNA polymerase beta' chain family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074861.
HOGENOMiHOG000205401.
InParanoidiP10964.
KOiK02999.
OMAiMGSYGRC.
OrthoDBiEOG72C57M.

Family and domain databases

InterProiIPR015699. DNA-dir_RNA_pol1_lsu.
IPR000722. RNA_pol_asu.
IPR006592. RNA_pol_N.
IPR007080. RNA_pol_Rpb1_1.
IPR007066. RNA_pol_Rpb1_3.
IPR007083. RNA_pol_Rpb1_4.
IPR007081. RNA_pol_Rpb1_5.
[Graphical view]
PANTHERiPTHR19376:SF11. PTHR19376:SF11. 3 hits.
PfamiPF04997. RNA_pol_Rpb1_1. 1 hit.
PF00623. RNA_pol_Rpb1_2. 1 hit.
PF04983. RNA_pol_Rpb1_3. 1 hit.
PF05000. RNA_pol_Rpb1_4. 1 hit.
PF04998. RNA_pol_Rpb1_5. 1 hit.
[Graphical view]
SMARTiSM00663. RPOLA_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10964-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDISKPVGSE ITSVDFGILT AKEIRNLSAK QITNPTVLDN LGHPVSGGLY
60 70 80 90 100
DLALGAFLRN LCSTCGLDEK FCPGHQGHIE LPVPCYNPLF FNQLYIYLRA
110 120 130 140 150
SCLFCHHFRL KSVEVHRYAC KLRLLQYGLI DESYKLDEIT LGSLNSSMYT
160 170 180 190 200
DDEAIEDNED EMDGEGSKQS KDISSTLLNE LKSKRSEYVD MAIAKALSDG
210 220 230 240 250
RTTERGSFTA TVNDERKKLV HEFHKKLLSR GKCDNCGMFS PKFRKDGFTK
260 270 280 290 300
IFETALNEKQ ITNNRVKGFI RQDMIKKQKQ AKKLDGSNEA SANDEESFDV
310 320 330 340 350
GRNPTTRPKT GSTYILSTEV KNILDTVFRK EQCVLQYVFH SRPNLSRKLV
360 370 380 390 400
KADSFFMDVL VVPPTRFRLP SKLGEEVHEN SQNQLLSKVL TTSLLIRDLN
410 420 430 440 450
DDLSKLQKDK VSLEDRRVIF SRLMNAFVTI QNDVNAFIDS TKAQGRTSGK
460 470 480 490 500
VPIPGVKQAL EKKEGLFRKH MMGKRVNYAA RSVISPDPNI ETNEIGVPPV
510 520 530 540 550
FAVKLTYPEP VTAYNIAELR QAVINGPDKW PGATQIQNED GSLVSLIGMS
560 570 580 590 600
VEQRKALANQ LLTPSSNVST HTLNKKVYRH IKNRDVVLMN RQPTLHKASM
610 620 630 640 650
MGHKVRVLPN EKTLRLHYAN TGAYNADFDG DEMNMHFPQN ENARAEALNL
660 670 680 690 700
ANTDSQYLTP TSGSPVRGLI QDHISAGVWL TSKDSFFTRE QYQQYIYGCI
710 720 730 740 750
RPEDGHTTRS KIVTLPPTIF KPYPLWTGKQ IITTVLLNVT PPDMPGINLI
760 770 780 790 800
SKNKIKNEYW GKGSLENEVL FKDGALLCGI LDKSQYGASK YGIVHSLHEV
810 820 830 840 850
YGPEVAAKVL SVLGRLFTNY ITATAFTCGM DDLRLTAEGN KWRTDILKTS
860 870 880 890 900
VDTGREAAAE VTNLDKDTPA DDPELLKRLQ EILRDNNKSG ILDAVTSSKV
910 920 930 940 950
NAITSQVVSK CVPDGTMKKF PCNSMQAMAL SGAKGSNVNV SQIMCLLGQQ
960 970 980 990 1000
ALEGRRVPVM VSGKTLPSFK PYETDAMAGG YVKGRFYSGI KPQEYYFHCM
1010 1020 1030 1040 1050
AGREGLIDTA VKTSRSGYLQ RCLTKQLEGV HVSYDNSIRD ADGTLVQFMY
1060 1070 1080 1090 1100
GGDAIDITKE SHMTQFEFCL DNYYALLKKY NPSALIEHLD VESALKYSKK
1110 1120 1130 1140 1150
TLKYRKKHSK EPHYKQSVKY DPVLAKYNPA KYLGSVSENF QDKLESFLDK
1160 1170 1180 1190 1200
NSKLFKSSDG VNEKKFRALM QLKYMRSLIN PGEAVGIIAS QSVGEPSTQM
1210 1220 1230 1240 1250
TLNTFHFAGH GAANVTLGIP RLREIVMTAS AAIKTPQMTL PIWNDVSDEQ
1260 1270 1280 1290 1300
ADTFCKSISK VLLSEVIDKV IVTETTGTSN TAGGNAARSY VIHMRFFDNN
1310 1320 1330 1340 1350
EYSEEYDVSK EELQNVISNQ FIHLLEAAIV KEIKKQKRTT GPDIGVAVPR
1360 1370 1380 1390 1400
LQTDVANSSS NSKRLEEDND EEQSHKKTKQ AVSYDEPDED EIETMREAEK
1410 1420 1430 1440 1450
SSDEEGIDSD KESDSDSEDE DVDMNEQINK SIVEANNNMN KVQRDRQSAI
1460 1470 1480 1490 1500
ISHHRFITKY NFDDESGKWC EFKLELAADT EKLLMVNIVE EICRKSIIRQ
1510 1520 1530 1540 1550
IPHIDRCVHP EPENGKRVLV TEGVNFQAMW DQEAFIDVDG ITSNDVAAVL
1560 1570 1580 1590 1600
KTYGVEAARN TIVNEINNVF SRYAISVSFR HLDLIADMMT RQGTYLAFNR
1610 1620 1630 1640 1650
QGMETSTSSF MKMSYETTCQ FLTKAVLDNE REQLDSPSAR IVVGKLNNVG
1660
TGSFDVLAKV PNAA
Length:1,664
Mass (Da):186,432
Last modified:November 1, 1997 - v2
Checksum:iDF65A7AA459D5E6D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti158 – 1581N → T in AAA34890 (PubMed:2830265).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03530 Genomic DNA. Translation: AAA34890.1.
X95720 Genomic DNA. Translation: CAA65029.1.
Z75249 Genomic DNA. Translation: CAA99665.1.
BK006948 Genomic DNA. Translation: DAA11102.1.
PIRiS67250.
RefSeqiNP_014986.3. NM_001183761.3.

Genome annotation databases

EnsemblFungiiYOR341W; YOR341W; YOR341W.
GeneIDi854519.
KEGGisce:YOR341W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03530 Genomic DNA. Translation: AAA34890.1.
X95720 Genomic DNA. Translation: CAA65029.1.
Z75249 Genomic DNA. Translation: CAA99665.1.
BK006948 Genomic DNA. Translation: DAA11102.1.
PIRiS67250.
RefSeqiNP_014986.3. NM_001183761.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C2MX-ray2.80A/P1-1664[»]
4C3HX-ray3.27A1-1664[»]
4C3IX-ray3.0A1-1664[»]
4C3JX-ray3.35A1-1664[»]
4YM7X-ray5.50AA/BA/CA/DA/EA/FA1-1664[»]
ProteinModelPortaliP10964.
SMRiP10964. Positions 1178-1209, 1438-1663.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34724. 112 interactions.
DIPiDIP-999N.
IntActiP10964. 37 interactions.
MINTiMINT-613626.

PTM databases

iPTMnetiP10964.

Proteomic databases

MaxQBiP10964.
PeptideAtlasiP10964.
TopDownProteomicsiP10964.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR341W; YOR341W; YOR341W.
GeneIDi854519.
KEGGisce:YOR341W.

Organism-specific databases

EuPathDBiFungiDB:YOR341W.
SGDiS000005868. RPA190.

Phylogenomic databases

GeneTreeiENSGT00550000074861.
HOGENOMiHOG000205401.
InParanoidiP10964.
KOiK02999.
OMAiMGSYGRC.
OrthoDBiEOG72C57M.

Enzyme and pathway databases

BioCyciYEAST:G3O-33816-MONOMER.

Miscellaneous databases

PROiP10964.

Family and domain databases

InterProiIPR015699. DNA-dir_RNA_pol1_lsu.
IPR000722. RNA_pol_asu.
IPR006592. RNA_pol_N.
IPR007080. RNA_pol_Rpb1_1.
IPR007066. RNA_pol_Rpb1_3.
IPR007083. RNA_pol_Rpb1_4.
IPR007081. RNA_pol_Rpb1_5.
[Graphical view]
PANTHERiPTHR19376:SF11. PTHR19376:SF11. 3 hits.
PfamiPF04997. RNA_pol_Rpb1_1. 1 hit.
PF00623. RNA_pol_Rpb1_2. 1 hit.
PF04983. RNA_pol_Rpb1_3. 1 hit.
PF05000. RNA_pol_Rpb1_4. 1 hit.
PF04998. RNA_pol_Rpb1_5. 1 hit.
[Graphical view]
SMARTiSM00663. RPOLA_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "RPA190, the gene coding for the largest subunit of yeast RNA polymerase A."
    Memet S., Gouy M., Marck C., Sentenac A., Buhler J.-M.
    J. Biol. Chem. 263:2830-2839(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Nucleotide sequence analysis of a 40 kb segment on the right arm of yeast chromosome XV reveals 18 open reading frames including a new pyruvate kinase and three homologues to chromosome I genes."
    Purnelle B., Goffeau A.
    Yeast 12:1475-1481(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 90843 / S288c / FY73.
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "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.
  6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "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-1636, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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-889, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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.
  10. "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.
  11. "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.
  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, 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 nameiRPA1_YEAST
AccessioniPrimary (citable) accession number: P10964
Secondary accession number(s): D6W336, Q99330
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 164 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2840 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.