RSA3_YEAST
ID RSA3_YEAST Reviewed; 220 AA.
AC Q05942; D6VYM1;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Ribosome assembly protein 3;
GN Name=RSA3; OrderedLocusNames=YLR221C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
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 [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 FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN PRE-RIBOSOMAL PARTICLES,
RP AND INTERACTION WITH DBP6.
RX PubMed=15126390; DOI=10.1534/genetics.166.4.1687;
RA de la Cruz J., Lacombe T., Deloche O., Linder P., Kressler D.;
RT "The putative RNA helicase Dbp6p functionally interacts with Rpl3p, Nop8p
RT and the novel trans-acting Factor Rsa3p during biogenesis of 60S ribosomal
RT subunits in Saccharomyces cerevisiae.";
RL Genetics 166:1687-1699(2004).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH DBP6; NOP8; URB1 AND URB2.
RX PubMed=17145778; DOI=10.1128/mcb.01523-06;
RA Rosado I.V., Dez C., Lebaron S., Caizergues-Ferrer M., Henry Y.,
RA de la Cruz J.;
RT "Characterization of Saccharomyces cerevisiae Npa2p (Urb2p) reveals a Low-
RT molecular-mass complex containing Dbp6p, Npa1p (Urb1p), Nop8p, and Rsa3p
RT involved in early steps of 60S ribosomal subunit biogenesis.";
RL Mol. Cell. Biol. 27:1207-1221(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND THR-88, AND
RP IDENTIFICATION BY 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).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Required for efficient biogenesis of the 60S ribosomal
CC subunit. {ECO:0000269|PubMed:15126390}.
CC -!- SUBUNIT: Associates with nucleolar pre-ribosomal particles. Interacts
CC with DBP6. Together with DBP6, NOP8, URB1 and URB2, forms an RNA-
CC independent complex, which is required during early maturation of
CC nascent 60S ribosomal subunits. {ECO:0000269|PubMed:15126390,
CC ECO:0000269|PubMed:17145778}.
CC -!- INTERACTION:
CC Q05942; P53734: DBP6; NbExp=3; IntAct=EBI-33602, EBI-5625;
CC Q05942; P34241: URB1; NbExp=4; IntAct=EBI-33602, EBI-26595;
CC Q05942; P47108: URB2; NbExp=5; IntAct=EBI-33602, EBI-25492;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15126390}.
CC -!- MISCELLANEOUS: Present with 2940 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RSA3 family. {ECO:0000305}.
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DR EMBL; U19027; AAB67410.1; -; Genomic_DNA.
DR EMBL; AY557937; AAS56263.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09537.1; -; Genomic_DNA.
DR PIR; S51444; S51444.
DR RefSeq; NP_013322.1; NM_001182108.1.
DR AlphaFoldDB; Q05942; -.
DR SMR; Q05942; -.
DR BioGRID; 31488; 132.
DR ComplexPortal; CPX-1421; NOP8 60s ribosome pre-assembly complex.
DR DIP; DIP-4421N; -.
DR IntAct; Q05942; 24.
DR MINT; Q05942; -.
DR STRING; 4932.YLR221C; -.
DR iPTMnet; Q05942; -.
DR MaxQB; Q05942; -.
DR PaxDb; Q05942; -.
DR PRIDE; Q05942; -.
DR EnsemblFungi; YLR221C_mRNA; YLR221C; YLR221C.
DR GeneID; 850918; -.
DR KEGG; sce:YLR221C; -.
DR SGD; S000004211; RSA3.
DR VEuPathDB; FungiDB:YLR221C; -.
DR eggNOG; ENOG502S5DP; Eukaryota.
DR HOGENOM; CLU_119118_0_0_1; -.
DR InParanoid; Q05942; -.
DR OMA; DAHNNNK; -.
DR BioCyc; YEAST:G3O-32335-MON; -.
DR PRO; PR:Q05942; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q05942; protein.
DR GO; GO:0005730; C:nucleolus; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IC:ComplexPortal.
DR InterPro; IPR028217; Rsa3_C.
DR Pfam; PF14615; Rsa3; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosome biogenesis.
FT CHAIN 1..220
FT /note="Ribosome assembly protein 3"
FT /id="PRO_0000097468"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 88
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 220 AA; 24656 MW; FCD901483337B8D6 CRC64;
MSAGDISAIN IKSVKKNRRR KKRRTADVSS SDSSSSDPSS ESEKEEIQNG AIEEHVGENG
KSDHVFSKGN DEDKQEDIAI EVSDVELTDE ESKDLKLNSK EVIDDLTKIS LSKIPEPTKS
QNKEGFMNAS KIAENIKLAR EEYNELAENF VPKGKDKTKL REEYLNLLFE NYGDDINRLR
AAPDFTNKSL SILADALQEG IGMFDIGELE LVLKNKEMEN
