RSA1_YEAST
ID RSA1_YEAST Reviewed; 381 AA.
AC Q08932; D6W3H5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Ribosome assembly 1 protein;
GN Name=RSA1; OrderedLocusNames=YPL193W;
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=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]
RP CHARACTERIZATION.
RX PubMed=10567587; DOI=10.1128/mcb.19.12.8633;
RA Kressler D., Doere M., Rojo M., Linder P.;
RT "Synthetic lethality with conditional dbp6 alleles identifies Rsa1p, a
RT nucleoplasmic protein involved in the assembly of 60S ribosomal subunits.";
RL Mol. Cell. Biol. 19:8633-8645(1999).
RN [4]
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]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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: Involved in a late nucleoplasmic step of 60S ribosomal
CC subunit assembly.
CC -!- INTERACTION:
CC Q08932; P46973: HIT1; NbExp=8; IntAct=EBI-16186, EBI-8359;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; Z73549; CAA97906.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11241.1; -; Genomic_DNA.
DR PIR; S65212; S65212.
DR RefSeq; NP_015131.1; NM_001184007.1.
DR PDB; 2M3F; NMR; -; A=238-259.
DR PDB; 2MJF; NMR; -; A=317-352.
DR PDB; 4NUT; X-ray; 1.55 A; B=238-290.
DR PDBsum; 2M3F; -.
DR PDBsum; 2MJF; -.
DR PDBsum; 4NUT; -.
DR AlphaFoldDB; Q08932; -.
DR BMRB; Q08932; -.
DR SMR; Q08932; -.
DR BioGRID; 35990; 43.
DR DIP; DIP-5698N; -.
DR IntAct; Q08932; 6.
DR STRING; 4932.YPL193W; -.
DR iPTMnet; Q08932; -.
DR MaxQB; Q08932; -.
DR PaxDb; Q08932; -.
DR PRIDE; Q08932; -.
DR EnsemblFungi; YPL193W_mRNA; YPL193W; YPL193W.
DR GeneID; 855908; -.
DR KEGG; sce:YPL193W; -.
DR SGD; S000006114; RSA1.
DR VEuPathDB; FungiDB:YPL193W; -.
DR eggNOG; ENOG502S1E3; Eukaryota.
DR HOGENOM; CLU_038609_0_0_1; -.
DR InParanoid; Q08932; -.
DR OMA; YCENTQA; -.
DR BioCyc; YEAST:G3O-34086-MON; -.
DR PRO; PR:Q08932; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08932; protein.
DR GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IMP:SGD.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
DR InterPro; IPR019496; NUFIP1_cons_dom.
DR Pfam; PF10453; NUFIP1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis.
FT CHAIN 1..381
FT /note="Ribosome assembly 1 protein"
FT /id="PRO_0000097460"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 240..256
FT /evidence="ECO:0007829|PDB:4NUT"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:4NUT"
FT HELIX 320..334
FT /evidence="ECO:0007829|PDB:2MJF"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:2MJF"
SQ SEQUENCE 381 AA; 43998 MW; 16058BA430E0F310 CRC64;
MNYNNFENSK GDGHSRLPKP TYSGTLSDGY DESKIKRQKT DSAFNAAYSP HMYPNSPYYE
GSWNTGYTPQ LHHVAPHNQY FHPIQPSTQY NYTSPPNYTE NYIPPVHQNI SYAPALNLQK
WPSSYCENTQ ALKNDKDYQT SISYEDVAIP TVKEIQLIEK NRGKDTFMNE ISPVPSSKDQ
ASAEPTEIPR KDPELANSNA EDDHNNLGLE DDDRDEQLES EGLGKVVLVP GTSIALITDE
DVKKWREERK KMWLLKISNN KQKHMQEMGI KEDELKSQPS IFKESRKEKQ FIQSIQNQVQ
RGNPKIDLNL KLIQREFANE NSQLLDFIRE LGDVGLLEYE LSQQEKDVLF GSSEDNNKNH
YKPNYKNRKP NLSRANFTRN K
