NSA2_YEAST
ID NSA2_YEAST Reviewed; 261 AA.
AC P40078; D3DM32;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Ribosome biogenesis protein NSA2;
DE AltName: Full=NOP7-associated protein 2;
GN Name=NSA2; OrderedLocusNames=YER126C; ORFNames=SYGP-ORF47;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 IDENTIFICATION IN THE PRE-66S RIBOSOMAL PARTICLE, INTERACTION WITH NOP7,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11583614; DOI=10.1016/s1097-2765(01)00344-6;
RA Harnpicharnchai P., Jakovljevic J., Horsey E., Miles T., Roman J., Rout M.,
RA Meagher D., Imai B., Guo Y., Brame C.J., Shabanowitz J., Hunt D.F.,
RA Woolford J.L. Jr.;
RT "Composition and functional characterization of yeast 66S ribosome assembly
RT intermediates.";
RL Mol. Cell 8:505-515(2001).
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 IDENTIFICATION IN THE PRE-66S RIBOSOMAL PARTICLE, INTERACTION WITH RRP1,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15100437; DOI=10.1261/rna.5255804;
RA Horsey E.W., Jakovljevic J., Miles T.D., Harnpicharnchai P.,
RA Woolford J.L. Jr.;
RT "Role of the yeast Rrp1 protein in the dynamics of pre-ribosome
RT maturation.";
RL RNA 10:813-827(2004).
RN [7]
RP FUNCTION, AND INTERACTION WITH NOG1.
RX PubMed=16861225; DOI=10.1074/jbc.m602199200;
RA Lebreton A., Saveanu C., Decourty L., Jacquier A., Fromont-Racine M.;
RT "Nsa2 is an unstable, conserved factor required for the maturation of 27 SB
RT pre-rRNAs.";
RL J. Biol. Chem. 281:27099-27108(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).
RN [9]
RP INTERACTION WITH NOP7, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17443350; DOI=10.1007/s00438-007-0233-1;
RA Fuentes J.L., Datta K., Sullivan S.M., Walker A., Maddock J.R.;
RT "In vivo functional characterization of the Saccharomyces cerevisiae 60S
RT biogenesis GTPase Nog1.";
RL Mol. Genet. Genomics 278:105-123(2007).
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).
RN [11]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.08 ANGSTROMS).
RX PubMed=27251291; DOI=10.1038/nature17942;
RA Wu S., Tutuncuoglu B., Yan K., Brown H., Zhang Y., Tan D., Gamalinda M.,
RA Yuan Y., Li Z., Jakovljevic J., Ma C., Lei J., Dong M.Q.,
RA Woolford J.L. Jr., Gao N.;
RT "Diverse roles of assembly factors revealed by structures of late nuclear
RT pre-60S ribosomes.";
RL Nature 534:133-137(2016).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 81-101, INTERACTION WITH RSA4,
RP AND MUTAGENESIS OF TYR-90.
RX PubMed=25404745; DOI=10.1083/jcb.201408111;
RA Bassler J., Paternoga H., Holdermann I., Thoms M., Granneman S.,
RA Barrio-Garcia C., Nyarko A., Lee W., Stier G., Clark S.A., Schraivogel D.,
RA Kallas M., Beckmann R., Tollervey D., Barbar E., Sinning I., Hurt E.;
RT "A network of assembly factors is involved in remodeling rRNA elements
RT during preribosome maturation.";
RL J. Cell Biol. 207:481-498(2014).
RN [13]
RP ERRATUM OF PUBMED:25404745.
RX PubMed=26150393; DOI=10.1083/jcb.20140811106112015c;
RA Bassler J., Paternoga H., Holdermann I., Thoms M., Granneman S.,
RA Barrio-Garcia C., Nyarko A., Lee W., Stier G., Clark S.A., Schraivogel D.,
RA Kallas M., Beckmann R., Tollervey D., Barbar E., Sinning I., Hurt E.;
RL J. Cell Biol. 210:169-170(2015).
CC -!- FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. May
CC play a part in the quality control of pre-60S particles. Under normal,
CC rapid growth conditions, high levels of NSA2 would allow the
CC progression of pre-60S particles through the ITS2 processing.
CC {ECO:0000269|PubMed:16544271, ECO:0000269|PubMed:16861225}.
CC -!- SUBUNIT: Component of the pre-66S ribosomal particle. Interacts with
CC NOP7 and RRP1. Interacts with RSA4 (via WD repeats) (PubMed:25404745).
CC {ECO:0000269|PubMed:11583614, ECO:0000269|PubMed:15100437,
CC ECO:0000269|PubMed:16861225, ECO:0000269|PubMed:17443350,
CC ECO:0000269|PubMed:25404745}.
CC -!- INTERACTION:
CC P40078; P53188: CGR1; NbExp=4; IntAct=EBI-22681, EBI-23731;
CC P40078; P36049: EBP2; NbExp=3; IntAct=EBI-22681, EBI-6289;
CC P40078; Q03532: HAS1; NbExp=3; IntAct=EBI-22681, EBI-8170;
CC P40078; P39744: NOC2; NbExp=3; IntAct=EBI-22681, EBI-29259;
CC P40078; Q02892: NOG1; NbExp=4; IntAct=EBI-22681, EBI-12105;
CC P40078; P53927: NOP15; NbExp=3; IntAct=EBI-22681, EBI-28853;
CC P40078; P53131: PRP43; NbExp=3; IntAct=EBI-22681, EBI-505;
CC P40078; P25382: RSA4; NbExp=4; IntAct=EBI-22681, EBI-21980;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 8660 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS8 family.
CC Ribosome biogenesis protein NSA2 subfamily. {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; U18916; AAC03224.1; -; Genomic_DNA.
DR EMBL; AY693192; AAT93211.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07786.1; -; Genomic_DNA.
DR PIR; S43218; S43218.
DR RefSeq; NP_011052.1; NM_001179016.1.
DR PDB; 3JCT; EM; 3.08 A; r=1-261.
DR PDB; 4WJV; X-ray; 3.20 A; I/J/K/L=81-101.
DR PDB; 6ELZ; EM; 3.30 A; r=1-261.
DR PDB; 6EM1; EM; 3.60 A; r=1-261.
DR PDB; 6EM5; EM; 4.30 A; r=1-261.
DR PDB; 6FT6; EM; 3.90 A; r=1-261.
DR PDB; 6M62; EM; 3.20 A; r=1-261.
DR PDB; 6N8J; EM; 3.50 A; r=1-261.
DR PDB; 7BT6; EM; 3.12 A; r=1-261.
DR PDB; 7BTB; EM; 3.22 A; r=1-261.
DR PDB; 7OF1; EM; 3.10 A; r=1-261.
DR PDB; 7OH3; EM; 3.40 A; r=1-261.
DR PDB; 7OHP; EM; 3.90 A; r=1-261.
DR PDB; 7OHQ; EM; 3.10 A; r=1-261.
DR PDB; 7OHR; EM; 4.72 A; r=1-261.
DR PDB; 7OHS; EM; 4.38 A; r=1-261.
DR PDB; 7OHT; EM; 4.70 A; r=1-261.
DR PDB; 7OHU; EM; 3.70 A; r=1-261.
DR PDB; 7OHV; EM; 3.90 A; r=1-261.
DR PDB; 7OHW; EM; 3.50 A; r=1-261.
DR PDB; 7OHY; EM; 3.90 A; r=1-261.
DR PDBsum; 3JCT; -.
DR PDBsum; 4WJV; -.
DR PDBsum; 6ELZ; -.
DR PDBsum; 6EM1; -.
DR PDBsum; 6EM5; -.
DR PDBsum; 6FT6; -.
DR PDBsum; 6M62; -.
DR PDBsum; 6N8J; -.
DR PDBsum; 7BT6; -.
DR PDBsum; 7BTB; -.
DR PDBsum; 7OF1; -.
DR PDBsum; 7OH3; -.
DR PDBsum; 7OHP; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHR; -.
DR PDBsum; 7OHS; -.
DR PDBsum; 7OHT; -.
DR PDBsum; 7OHU; -.
DR PDBsum; 7OHV; -.
DR PDBsum; 7OHW; -.
DR PDBsum; 7OHY; -.
DR AlphaFoldDB; P40078; -.
DR SMR; P40078; -.
DR BioGRID; 36870; 100.
DR DIP; DIP-1892N; -.
DR IntAct; P40078; 42.
DR MINT; P40078; -.
DR STRING; 4932.YER126C; -.
DR MaxQB; P40078; -.
DR PaxDb; P40078; -.
DR PRIDE; P40078; -.
DR EnsemblFungi; YER126C_mRNA; YER126C; YER126C.
DR GeneID; 856863; -.
DR KEGG; sce:YER126C; -.
DR SGD; S000000928; NSA2.
DR VEuPathDB; FungiDB:YER126C; -.
DR eggNOG; KOG3163; Eukaryota.
DR GeneTree; ENSGT00390000018706; -.
DR HOGENOM; CLU_1070048_0_0_1; -.
DR InParanoid; P40078; -.
DR OMA; TKSWKRM; -.
DR BioCyc; YEAST:G3O-30289-MON; -.
DR PRO; PR:P40078; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40078; protein.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA: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 GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR CDD; cd11381; NSA2; 1.
DR InterPro; IPR039411; NSA2_fam.
DR InterPro; IPR022309; Ribosomal_S8e/biogenesis_NSA2.
DR PANTHER; PTHR12642; PTHR12642; 1.
DR Pfam; PF01201; Ribosomal_S8e; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Ribosome biogenesis;
KW rRNA processing.
FT CHAIN 1..261
FT /note="Ribosome biogenesis protein NSA2"
FT /id="PRO_0000202648"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..98
FT /note="Interaction with RSA4"
FT /evidence="ECO:0000269|PubMed:25404745"
FT MOTIF 15..22
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 51..58
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 7..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 90
FT /note="Y->A: Abolishes interaction with RSA4. Blocks
FT production of mature 60S subunits, and causes the
FT accumulation of pre-60S particles."
FT /evidence="ECO:0000269|PubMed:25404745"
FT TURN 89..93
FT /evidence="ECO:0007829|PDB:4WJV"
SQ SEQUENCE 261 AA; 29723 MW; 545C8B4250BCB0C9 CRC64;
MPQNDYIERH IKQHGKRLDH EERKRKREAR ESHKISERAQ KLTGWKGKQF AKKRYAEKVS
MRKKIKAHEQ SKVKGSSKPL DTDGDALPTY LLDREQNNTA KAISSSIKQK RLEKADKFSV
PLPKVRGISE EEMFKVIKTG KSRSKSWKRM ITKHTFVGEG FTRRPVKMER IIRPSALRQK
KANVTHPELG VTVFLPILAV KKNPQSPMYT QLGVLTKGTI IEVNVSELGM VTAGGKVVWG
KYAQVTNEPD RDGCVNAVLL V
