RPF2_YEAST
ID RPF2_YEAST Reviewed; 344 AA.
AC P36160; D6VXE1;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Ribosome biogenesis protein RPF2;
GN Name=RPF2; OrderedLocusNames=YKR081C; ORFNames=YKR401;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8203164; DOI=10.1002/yea.320100210;
RA Garcia-Cantalejo J.M., Baladron V., Esteban P.F., Santos M.A., Bou G.,
RA Remacha M.A., Revuelta J.L., Ballesta J.P.G., Jimenez A., del Rey F.;
RT "The complete sequence of an 18,002 bp segment of Saccharomyces cerevisiae
RT chromosome XI contains the HBS1, MRP-L20 and PRP16 genes, and six new open
RT reading frames.";
RL Yeast 10:231-245(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12702244; DOI=10.1111/j.1567-1364.2003.tb00136.x;
RA Bogengruber E., Briza P., Doppler E., Wimmer H., Koller L., Fasiolo F.,
RA Senger B., Hegemann J.H., Breitenbach M.;
RT "Functional analysis in yeast of the Brix protein superfamily involved in
RT the biogenesis of ribosomes.";
RL FEMS Yeast Res. 3:35-43(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
CC -!- FUNCTION: Required for biogenesis of the 60S ribosomal subunit.
CC {ECO:0000269|PubMed:12702244}.
CC -!- SUBUNIT: Part of a complex that includes BRX1, RPF1, RPF2 and SSF1 or
CC SSF2.
CC -!- INTERACTION:
CC P36160; Q12176: MAK21; NbExp=5; IntAct=EBI-15881, EBI-10944;
CC P36160; P39744: NOC2; NbExp=6; IntAct=EBI-15881, EBI-29259;
CC P36160; Q02892: NOG1; NbExp=6; IntAct=EBI-15881, EBI-12105;
CC P36160; P40010: NUG1; NbExp=6; IntAct=EBI-15881, EBI-22449;
CC P36160; Q08746: RRS1; NbExp=5; IntAct=EBI-15881, EBI-16026;
CC P36160; P25582: SPB1; NbExp=6; IntAct=EBI-15881, EBI-17814;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12702244}.
CC -!- MISCELLANEOUS: Present with 32400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RPF2 family. {ECO:0000305}.
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DR EMBL; Z27116; CAA81632.1; -; Genomic_DNA.
DR EMBL; Z28306; CAA82160.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09231.1; -; Genomic_DNA.
DR PIR; S38159; S38159.
DR RefSeq; NP_013007.1; NM_001179871.1.
DR PDB; 3JCT; EM; 3.08 A; v=1-344.
DR PDB; 5A53; X-ray; 2.40 A; C=23-252.
DR PDB; 5WXL; X-ray; 1.90 A; A/C=19-288.
DR PDB; 6FT6; EM; 3.90 A; v=1-344.
DR PDB; 6M62; EM; 3.20 A; v=1-254.
DR PDB; 7BT6; EM; 3.12 A; v=1-344.
DR PDB; 7BTB; EM; 3.22 A; v=1-344.
DR PDB; 7OH3; EM; 3.40 A; v=1-344.
DR PDB; 7OHQ; EM; 3.10 A; v=1-344.
DR PDB; 7OHT; EM; 4.70 A; v=1-344.
DR PDBsum; 3JCT; -.
DR PDBsum; 5A53; -.
DR PDBsum; 5WXL; -.
DR PDBsum; 6FT6; -.
DR PDBsum; 6M62; -.
DR PDBsum; 7BT6; -.
DR PDBsum; 7BTB; -.
DR PDBsum; 7OH3; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHT; -.
DR AlphaFoldDB; P36160; -.
DR SMR; P36160; -.
DR BioGRID; 34212; 485.
DR DIP; DIP-6602N; -.
DR IntAct; P36160; 297.
DR MINT; P36160; -.
DR STRING; 4932.YKR081C; -.
DR iPTMnet; P36160; -.
DR MaxQB; P36160; -.
DR PaxDb; P36160; -.
DR PRIDE; P36160; -.
DR EnsemblFungi; YKR081C_mRNA; YKR081C; YKR081C.
DR GeneID; 853956; -.
DR KEGG; sce:YKR081C; -.
DR SGD; S000001789; RPF2.
DR VEuPathDB; FungiDB:YKR081C; -.
DR eggNOG; KOG3031; Eukaryota.
DR GeneTree; ENSGT00390000007279; -.
DR HOGENOM; CLU_049783_0_0_1; -.
DR InParanoid; P36160; -.
DR OMA; GCKIPRI; -.
DR BioCyc; YEAST:G3O-32044-MON; -.
DR PRO; PR:P36160; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36160; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; HDA:SGD.
DR GO; GO:0008097; F:5S rRNA binding; IDA:SGD.
DR GO; GO:0008312; F:7S RNA binding; IDA:SGD.
DR GO; GO:0019843; F:rRNA binding; IDA:SGD.
DR GO; GO:1902626; P:assembly of large subunit precursor of preribosome; IMP:SGD.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
DR InterPro; IPR007109; Brix.
DR InterPro; IPR039770; Rpf2.
DR PANTHER; PTHR12728; PTHR12728; 1.
DR Pfam; PF04427; Brix; 1.
DR SMART; SM00879; Brix; 1.
DR PROSITE; PS50833; BRIX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..344
FT /note="Ribosome biogenesis protein RPF2"
FT /id="PRO_0000120256"
FT DOMAIN 28..243
FT /note="Brix"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00034"
FT REGION 291..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..331
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:5WXL"
FT HELIX 40..53
FT /evidence="ECO:0007829|PDB:5WXL"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:5WXL"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:5WXL"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:5WXL"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:5WXL"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:5WXL"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:5WXL"
FT STRAND 109..118
FT /evidence="ECO:0007829|PDB:5WXL"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:5WXL"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:5WXL"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:5WXL"
FT HELIX 152..165
FT /evidence="ECO:0007829|PDB:5WXL"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:5WXL"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:5WXL"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:5WXL"
FT STRAND 199..209
FT /evidence="ECO:0007829|PDB:5WXL"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:5WXL"
FT STRAND 229..238
FT /evidence="ECO:0007829|PDB:5WXL"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:5WXL"
SQ SEQUENCE 344 AA; 39599 MW; 4ACE390E6B1700EA CRC64;
MIRTVKPKNA RAKRALVKRE AKLVENVKQA LFIPGQSCNK NLHDIMVDLS ALKKPDMKRF
NRKNDIHPFE DMSPLEFFSE KNDCSLMVLM TSSKKRKNNM TFIRTFGYKI YDMIELMVAD
NFKLLSDFKK LTFTVGLKPM FTFQGAAFDT HPVYKQIKSL FLDFFRGEST DLQDVAGLQH
VISMTIQGDF QDGEPLPNVL FRVYKLKSYK SDQGGKRLPR IELVEIGPRL DFKIGRIHTP
SPDMVTEAHK KPKQLEMKTK KNVELDIMGD KLGRIHMGKQ DLGKLQTRKM KGLKSKFDQG
TEEGDGEVDE DYEDEASYSD DGQEYEEEFV SATDIEPSAK RQKK
