RRP15_YEAST
ID RRP15_YEAST Reviewed; 250 AA.
AC Q06511; D6W4E0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Ribosomal RNA-processing protein 15;
GN Name=RRP15 {ECO:0000312|SGD:S000006347}; OrderedLocusNames=YPR143W;
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] {ECO:0000312|EMBL:AAB68282.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4] {ECO:0000305}
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 [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=15769876; DOI=10.1261/rna.7200205;
RA De Marchis M.L., Giorgi A., Schinina M.E., Bozzoni I., Fatica A.;
RT "Rrp15p, a novel component of pre-ribosomal particles required for 60S
RT ribosome subunit maturation.";
RL RNA 11:495-502(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, 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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Constituent of pre-60S ribosomal particles. Required for
CC large subunit rRNA maturation, in particular processing of the 27S pre-
CC rRNA at the A3 and B1 sites to yield 5.8S and 25S rRNA.
CC {ECO:0000269|PubMed:15769876}.
CC -!- INTERACTION:
CC Q06511; P20484: MAK11; NbExp=3; IntAct=EBI-34602, EBI-10930;
CC Q06511; Q12176: MAK21; NbExp=4; IntAct=EBI-34602, EBI-10944;
CC Q06511; P38789: SSF1; NbExp=4; IntAct=EBI-34602, EBI-18160;
CC Q06511; Q12153: SSF2; NbExp=5; IntAct=EBI-34602, EBI-18168;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 6200 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RRP15 family. {ECO:0000305}.
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DR EMBL; U40829; AAB68282.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11556.1; -; Genomic_DNA.
DR PIR; S69031; S69031.
DR RefSeq; NP_015469.1; NM_001184240.1.
DR PDB; 6C0F; EM; 3.70 A; w=1-250.
DR PDBsum; 6C0F; -.
DR AlphaFoldDB; Q06511; -.
DR SMR; Q06511; -.
DR BioGRID; 36311; 158.
DR DIP; DIP-6432N; -.
DR IntAct; Q06511; 13.
DR MINT; Q06511; -.
DR STRING; 4932.YPR143W; -.
DR iPTMnet; Q06511; -.
DR MaxQB; Q06511; -.
DR PaxDb; Q06511; -.
DR PRIDE; Q06511; -.
DR EnsemblFungi; YPR143W_mRNA; YPR143W; YPR143W.
DR GeneID; 856264; -.
DR KEGG; sce:YPR143W; -.
DR SGD; S000006347; RRP15.
DR VEuPathDB; FungiDB:YPR143W; -.
DR eggNOG; KOG2974; Eukaryota.
DR HOGENOM; CLU_058264_0_0_1; -.
DR InParanoid; Q06511; -.
DR OMA; FVKQRFY; -.
DR BioCyc; YEAST:G3O-34277-MON; -.
DR PRO; PR:Q06511; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06511; protein.
DR GO; GO:0005730; C:nucleolus; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IBA:GO_Central.
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:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR InterPro; IPR012459; Rrp15.
DR PANTHER; PTHR13245; PTHR13245; 1.
DR Pfam; PF07890; Rrp15p; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; rRNA processing.
FT CHAIN 1..250
FT /note="Ribosomal RNA-processing protein 15"
FT /id="PRO_0000270562"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 250 AA; 28212 MW; 23E401BB1B82470C CRC64;
MGSKHRVDTK DKKRTRKNAE FGREKRNSGN QELSNEPEKD TIMEGDEAEE DEQNSSSDES
SKIIDNEQSD AEEDDDEEEE DDDFPRKKKS KNSKHDDGST GFSAAVNAIL SSHLKAYDRK
DPIMARNKKV LKQSESEKLE YKAKKALLAE KKKLLGKARK TDIIPIASGE DRSENIRKVL
EKETALRKIA QKGAVKLFNA ILATQVKTEK EVSENLSEIK NKEEKKELIT EVSKEKFLDL
VKAAAGSDNE
