ID RL1D1_YEAST Reviewed; 274 AA. AC P36144; D6VXC1; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 27-MAR-2024, entry version 163. DE RecName: Full=Ribosome biogenesis protein UTP30; DE AltName: Full=U3 snoRNP-associated protein UTP30; GN Name=UTP30; OrderedLocusNames=YKR060W; 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=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 [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 IDENTIFICATION IN THE 90S PRE-RIBOSOME, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=12150911; DOI=10.1016/s1097-2765(02)00579-8; RA Grandi P., Rybin V., Bassler J., Petfalski E., Strauss D., Marzioch M., RA Schaefer T., Kuster B., Tschochner H., Tollervey D., Gavin A.-C., Hurt E.; RT "90S pre-ribosomes include the 35S pre-rRNA, the U3 snoRNP, and 40S subunit RT processing factors but predominantly lack 60S synthesis factors."; RL Mol. Cell 10:105-115(2002). RN [5] 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 [6] 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 [7] RP INTERACTION WITH FAF1. RX PubMed=16762320; DOI=10.1016/j.bbrc.2006.05.140; RA Rempola B., Karkusiewicz I., Piekarska I., Rytka J.; RT "Fcf1p and Fcf2p are novel nucleolar Saccharomyces cerevisiae proteins RT involved in pre-rRNA processing."; RL Biochem. Biophys. Res. Commun. 346:546-554(2006). RN [8] RP FUNCTION. RX PubMed=16544271; DOI=10.1002/yea.1353; RA Wade C.H., Umbarger M.A., McAlear M.A.; RT "The budding yeast rRNA and ribosome biosynthesis (RRB) regulon contains RT over 200 genes."; RL Yeast 23:293-306(2006). CC -!- FUNCTION: Involved in rRNA-processing and ribosome biosynthesis. CC {ECO:0000269|PubMed:16544271}. CC -!- SUBUNIT: Component of the 90S pre-ribosomes. Interacts with FAF1. CC {ECO:0000269|PubMed:12150911, ECO:0000269|PubMed:16762320}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 3060 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family. CC Highly divergent. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z28285; CAA82139.1; -; Genomic_DNA. DR EMBL; AY557907; AAS56233.1; -; Genomic_DNA. DR EMBL; BK006944; DAA09211.1; -; Genomic_DNA. DR PIR; S38136; S38136. DR RefSeq; NP_012986.1; NM_001179850.1. DR PDB; 5WLC; EM; 3.80 A; SN=1-274. DR PDB; 5WYJ; EM; 8.70 A; U5=1-274. DR PDB; 5WYK; EM; 4.50 A; U5=1-274. DR PDB; 5YDT; EM; 4.50 A; U5=1-274. DR PDB; 5YDU; X-ray; 2.65 A; A/B=1-274. DR PDB; 6KE6; EM; 3.40 A; RI=1-274. DR PDB; 6LQP; EM; 3.20 A; RI=1-274. DR PDB; 6LQU; EM; 3.70 A; RI=1-274. DR PDB; 6ZQA; EM; 4.40 A; UZ=1-274. DR PDB; 6ZQB; EM; 3.90 A; UZ=1-274. DR PDB; 6ZQC; EM; 3.80 A; UZ=1-274. DR PDB; 7AJT; EM; 4.60 A; UZ=1-274. DR PDB; 7D5S; EM; 4.60 A; RI=1-274. DR PDB; 7SUK; EM; 3.99 A; SN=11-257. DR PDBsum; 5WLC; -. DR PDBsum; 5WYJ; -. DR PDBsum; 5WYK; -. DR PDBsum; 5YDT; -. DR PDBsum; 5YDU; -. DR PDBsum; 6KE6; -. DR PDBsum; 6LQP; -. DR PDBsum; 6LQU; -. DR PDBsum; 6ZQA; -. DR PDBsum; 6ZQB; -. DR PDBsum; 6ZQC; -. DR PDBsum; 7AJT; -. DR PDBsum; 7D5S; -. DR PDBsum; 7SUK; -. DR AlphaFoldDB; P36144; -. DR EMDB; EMD-0949; -. DR EMDB; EMD-0954; -. DR EMDB; EMD-11357; -. DR EMDB; EMD-11358; -. DR EMDB; EMD-11359; -. DR EMDB; EMD-11807; -. DR EMDB; EMD-25441; -. DR EMDB; EMD-30584; -. DR EMDB; EMD-6695; -. DR EMDB; EMD-6696; -. DR EMDB; EMD-8859; -. DR EMDB; EMD-9964; -. DR SMR; P36144; -. DR BioGRID; 34191; 157. DR ComplexPortal; CPX-1604; Small ribosomal subunit processome. DR DIP; DIP-1926N; -. DR IntAct; P36144; 18. DR MINT; P36144; -. DR STRING; 4932.YKR060W; -. DR iPTMnet; P36144; -. DR MaxQB; P36144; -. DR PaxDb; 4932-YKR060W; -. DR PeptideAtlas; P36144; -. DR EnsemblFungi; YKR060W_mRNA; YKR060W; YKR060W. DR GeneID; 853934; -. DR KEGG; sce:YKR060W; -. DR AGR; SGD:S000001768; -. DR SGD; S000001768; UTP30. DR VEuPathDB; FungiDB:YKR060W; -. DR eggNOG; KOG1685; Eukaryota. DR HOGENOM; CLU_063901_0_0_1; -. DR InParanoid; P36144; -. DR OMA; CLTVRIG; -. DR OrthoDB; 103361at2759; -. DR BioCyc; YEAST:G3O-32028-MONOMER; -. DR BioGRID-ORCS; 853934; 1 hit in 10 CRISPR screens. DR PRO; PR:P36144; -. DR Proteomes; UP000002311; Chromosome XI. DR RNAct; P36144; Protein. DR GO; GO:0030686; C:90S preribosome; IDA:GO_Central. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0005730; C:nucleolus; IDA:GO_Central. DR GO; GO:0005634; C:nucleus; HDA:SGD. DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central. DR GO; GO:0030490; P:maturation of SSU-rRNA; NAS:ComplexPortal. DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IGI:GO_Central. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IPI:SGD. DR InterPro; IPR023674; Ribosomal_uL1-like. DR InterPro; IPR028364; Ribosomal_uL1/biogenesis. DR Pfam; PF00687; Ribosomal_L1; 1. DR SUPFAM; SSF56808; Ribosomal protein L1; 1. PE 1: Evidence at protein level; KW 3D-structure; Nucleus; Reference proteome; Ribosome biogenesis; KW rRNA processing. FT CHAIN 1..274 FT /note="Ribosome biogenesis protein UTP30" FT /id="PRO_0000203217" FT HELIX 12..26 FT /evidence="ECO:0007829|PDB:5YDU" FT HELIX 28..30 FT /evidence="ECO:0007829|PDB:5YDU" FT STRAND 35..44 FT /evidence="ECO:0007829|PDB:5YDU" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:5YDU" FT HELIX 67..69 FT /evidence="ECO:0007829|PDB:5YDU" FT STRAND 72..79 FT /evidence="ECO:0007829|PDB:5YDU" FT HELIX 81..88 FT /evidence="ECO:0007829|PDB:5YDU" FT TURN 91..96 FT /evidence="ECO:0007829|PDB:5YDU" FT STRAND 98..102 FT /evidence="ECO:0007829|PDB:5YDU" FT HELIX 103..109 FT /evidence="ECO:0007829|PDB:5YDU" FT HELIX 112..116 FT /evidence="ECO:0007829|PDB:5YDU" FT STRAND 123..128 FT /evidence="ECO:0007829|PDB:5YDU" FT HELIX 129..134 FT /evidence="ECO:0007829|PDB:5YDU" FT STRAND 152..154 FT /evidence="ECO:0007829|PDB:5YDU" FT HELIX 173..185 FT /evidence="ECO:0007829|PDB:5YDU" FT STRAND 186..189 FT /evidence="ECO:0007829|PDB:5YDU" FT STRAND 195..204 FT /evidence="ECO:0007829|PDB:5YDU" FT HELIX 209..223 FT /evidence="ECO:0007829|PDB:5YDU" FT HELIX 226..228 FT /evidence="ECO:0007829|PDB:5YDU" FT TURN 229..231 FT /evidence="ECO:0007829|PDB:5YDU" FT STRAND 239..245 FT /evidence="ECO:0007829|PDB:5YDU" FT STRAND 247..249 FT /evidence="ECO:0007829|PDB:5YDU" FT STRAND 252..255 FT /evidence="ECO:0007829|PDB:5YDU" SQ SEQUENCE 274 AA; 31616 MW; 897F2B8C54CE8030 CRC64; MVESNDIIKS GLAEKALKAL ILQCEENPSL KNDKDIHIII NTGKKMGINR DNIPRIIPLT KYKLFKPRDL NILLITKDPS ALYRETLTKD EHTSELFKEI ISVKNLRRRF KGSKLTQLYK DFDLVVADYR VHHLLPEVLG SRFYHGSKKL PYMIRMSKEV KLKRQQMVEK CDPIYVRAQL RSICKNTSYI PNNDNCLSVR VGYIQKHSIP EILQNIQDTI NFLTDKSKRP QGGVIKGGII SIFVKTSNST SLPIYQFSEA RENQKNEDLS DIKL //