ID   SNU13_YEAST             Reviewed;         126 AA.
AC   P39990; D3DLM2;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 196.
DE   RecName: Full=13 kDa ribonucleoprotein-associated protein;
DE   AltName: Full=Small nuclear ribonucleoprotein-associated protein 1;
GN   Name=SNU13; OrderedLocusNames=YEL026W;
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   SUBUNIT, IDENTIFICATION IN THE U4/U5/U6 TRI-SNRNP COMPLEX, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=10449419; DOI=10.1093/emboj/18.16.4535;
RA   Gottschalk A., Neubauer G., Banroques J., Mann M., Luehrmann R.,
RA   Fabrizio P.;
RT   "Identification by mass spectrometry and functional analysis of novel
RT   proteins of the yeast [U4/U6.U5] tri-snRNP.";
RL   EMBO J. 18:4535-4548(1999).
RN   [5]
RP   IDENTIFICATION IN U4/U6.U5 TRI-SNRNP COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=10377396; DOI=10.1073/pnas.96.13.7226;
RA   Stevens S.W., Abelson J.;
RT   "Purification of the yeast U4/U6.U5 small nuclear ribonucleoprotein
RT   particle and identification of its proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:7226-7231(1999).
RN   [6]
RP   FUNCTION, IDENTIFICATION IN U3 SNORNP, IDENTIFICATION BY MASS SPECTROMETRY,
RP   AND RNA-BINDING.
RX   PubMed=11081632; DOI=10.1016/s0092-8674(00)00137-9;
RA   Watkins N.J., Segault V., Charpentier B., Nottrott S., Fabrizio P.,
RA   Bachi A., Wilm M., Rosbash M., Branlant C., Luehrmann R.;
RT   "A common core RNP structure shared between the small nucleoar box C/D RNPs
RT   and the spliceosomal U4 snRNP.";
RL   Cell 103:457-466(2000).
RN   [7]
RP   IDENTIFICATION IN U1.U2.U4/U6.U5 PENTA-SNRNP COMPLEX, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=11804584; DOI=10.1016/s1097-2765(02)00436-7;
RA   Stevens S.W., Ryan D.E., Ge H.Y., Moore R.E., Young M.K., Lee T.D.,
RA   Abelson J.;
RT   "Composition and functional characterization of the yeast spliceosomal
RT   penta-snRNP.";
RL   Mol. Cell 9:31-44(2002).
RN   [8]
RP   FUNCTION, IDENTIFICATION IN U3 SNORNP, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=12215523; DOI=10.1128/mcb.22.19.6663-6668.2002;
RA   Galardi S., Fatica A., Bachi A., Scaloni A., Presutti C., Bozzoni I.;
RT   "Purified box C/D snoRNPs are able to reproduce site-specific 2'-O-
RT   methylation of target RNA in vitro.";
RL   Mol. Cell. Biol. 22:6663-6668(2002).
RN   [9]
RP   IDENTIFICATION IN SSU PROCESSOME BY MASS SPECTROMETRY.
RX   PubMed=12068309; DOI=10.1038/nature00769;
RA   Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M.,
RA   Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E., Shabanowitz J.,
RA   Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.;
RT   "A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA
RT   biogenesis.";
RL   Nature 417:967-970(2002).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA   Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA   Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA   Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT   "Assigning function to yeast proteins by integration of technologies.";
RL   Mol. Cell 12:1353-1365(2003).
RN   [11]
RP   RNA-BINDING.
RX   PubMed=12810916; DOI=10.1261/rna.2130503;
RA   Marmier-Gourrier N., Clery A., Senty-Segault V., Charpentier B.,
RA   Schlotter F., Leclerc F., Fournier R., Branlant C.;
RT   "A structural, phylogenetic, and functional study of 15.5-kD/Snu13 protein
RT   binding on U3 small nucleolar RNA.";
RL   RNA 9:821-838(2003).
RN   [12]
RP   FUNCTION, MUTAGENESIS OF GLU-59; VAL-81 AND ARG-84, AND RNA-BINDING.
RX   PubMed=14730029; DOI=10.1261/rna.5970404;
RA   Dobbyn H.C., O'Keefe R.T.;
RT   "Analysis of Snu13p mutations reveals differential interactions with the U4
RT   snRNA and U3 snoRNA.";
RL   RNA 10:308-320(2004).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX   PubMed=15963469; DOI=10.1016/j.bbrc.2005.05.141;
RA   Oruganti S., Zhang Y., Li H.;
RT   "Structural comparison of yeast snoRNP and spliceosomal protein Snu13p with
RT   its homologs.";
RL   Biochem. Biophys. Res. Commun. 333:550-554(2005).
CC   -!- FUNCTION: Common component of the spliceosome and rRNA processing
CC       machinery. In association with the spliceosomal U4/U6.U5 tri-snRNP
CC       particle, required for splicing of pre-mRNA. In association with box
CC       C/D snoRNPs, required for processing of pre-ribosomal RNA (rRNA) and
CC       site-specific 2'-O-methylation of substrate RNAs. Essential for the
CC       accumulation and stability of U4 snRNA, U6 snRNA, and box C/D snoRNAs.
CC       {ECO:0000269|PubMed:11081632, ECO:0000269|PubMed:12215523,
CC       ECO:0000269|PubMed:14730029}.
CC   -!- SUBUNIT: Binds to the C'/D and B/C motifs in U3 snoRNA. Component of
CC       the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and
CC       at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23,
CC       SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3,
CC       LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1. Binds to the 5'-stem-loop
CC       of U4 snRNA. Component of the ribosomal small subunit (SSU) processome
CC       composed of at least 40 protein subunits and snoRNA U3.
CC       {ECO:0000269|PubMed:10377396, ECO:0000269|PubMed:10449419,
CC       ECO:0000269|PubMed:11081632, ECO:0000269|PubMed:11804584,
CC       ECO:0000269|PubMed:12068309, ECO:0000269|PubMed:12215523}.
CC   -!- INTERACTION:
CC       P39990; P15646: NOP1; NbExp=6; IntAct=EBI-12032, EBI-6838;
CC       P39990; Q12460: NOP56; NbExp=4; IntAct=EBI-12032, EBI-17148;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family.
CC       {ECO:0000305}.
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DR   EMBL; U18530; AAB64503.1; -; Genomic_DNA.
DR   EMBL; AY558377; AAS56703.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07626.1; -; Genomic_DNA.
DR   PIR; S50433; S50433.
DR   RefSeq; NP_010888.1; NM_001178841.1.
DR   PDB; 1ZWZ; X-ray; 1.90 A; A/B=1-126.
DR   PDB; 2ALE; X-ray; 1.80 A; A=1-126.
DR   PDB; 3JCM; EM; 3.80 A; M=1-126.
DR   PDB; 4NUT; X-ray; 1.55 A; A=1-126.
DR   PDB; 5GAN; EM; 3.60 A; K=1-126.
DR   PDB; 5GAP; EM; 3.60 A; K=1-126.
DR   PDB; 5NRL; EM; 7.20 A; K=1-126.
DR   PDB; 5TZS; EM; 5.10 A; e/f=1-126.
DR   PDB; 5WLC; EM; 3.80 A; SE/SF=1-126.
DR   PDB; 5WYJ; EM; 8.70 A; 3G/3H=1-126.
DR   PDB; 5WYK; EM; 4.50 A; 3G/3H=1-126.
DR   PDB; 5ZWM; EM; 3.40 A; M=1-126.
DR   PDB; 5ZWO; EM; 3.90 A; M=1-126.
DR   PDB; 6KE6; EM; 3.40 A; 3G/3H=1-126.
DR   PDB; 6LQP; EM; 3.20 A; 3G/3H=1-126.
DR   PDB; 6LQQ; EM; 4.10 A; 3G/3H=1-126.
DR   PDB; 6LQR; EM; 8.60 A; 3G/3H=1-126.
DR   PDB; 6LQS; EM; 3.80 A; 3G/3H=1-126.
DR   PDB; 6LQT; EM; 4.90 A; 3G/3H=1-126.
DR   PDB; 6LQU; EM; 3.70 A; 3G/3H=1-126.
DR   PDB; 6LQV; EM; 4.80 A; 3G/3H=1-126.
DR   PDB; 6ND4; EM; 4.30 A; e/f=1-126.
DR   PDB; 6ZQA; EM; 4.40 A; CF/CG=1-126.
DR   PDB; 6ZQB; EM; 3.90 A; CF/CG=1-126.
DR   PDB; 6ZQC; EM; 3.80 A; CF/CG=1-126.
DR   PDB; 6ZQD; EM; 3.80 A; CF/CG=1-126.
DR   PDB; 6ZQE; EM; 7.10 A; CF/CG=1-126.
DR   PDB; 7AJT; EM; 4.60 A; CF/CG=1-126.
DR   PDB; 7AJU; EM; 3.80 A; CF/CG=1-126.
DR   PDB; 7D4I; EM; 4.00 A; 3G/3H=1-126.
DR   PDB; 7D5S; EM; 4.60 A; 3G/3H=1-126.
DR   PDB; 7D5T; EM; 6.00 A; 3G/3H=1-126.
DR   PDB; 7D63; EM; 12.30 A; 3G/3H=1-126.
DR   PDB; 7SUK; EM; 3.99 A; SE/SF=5-125.
DR   PDBsum; 1ZWZ; -.
DR   PDBsum; 2ALE; -.
DR   PDBsum; 3JCM; -.
DR   PDBsum; 4NUT; -.
DR   PDBsum; 5GAN; -.
DR   PDBsum; 5GAP; -.
DR   PDBsum; 5NRL; -.
DR   PDBsum; 5TZS; -.
DR   PDBsum; 5WLC; -.
DR   PDBsum; 5WYJ; -.
DR   PDBsum; 5WYK; -.
DR   PDBsum; 5ZWM; -.
DR   PDBsum; 5ZWO; -.
DR   PDBsum; 6KE6; -.
DR   PDBsum; 6LQP; -.
DR   PDBsum; 6LQQ; -.
DR   PDBsum; 6LQR; -.
DR   PDBsum; 6LQS; -.
DR   PDBsum; 6LQT; -.
DR   PDBsum; 6LQU; -.
DR   PDBsum; 6LQV; -.
DR   PDBsum; 6ND4; -.
DR   PDBsum; 6ZQA; -.
DR   PDBsum; 6ZQB; -.
DR   PDBsum; 6ZQC; -.
DR   PDBsum; 6ZQD; -.
DR   PDBsum; 6ZQE; -.
DR   PDBsum; 7AJT; -.
DR   PDBsum; 7AJU; -.
DR   PDBsum; 7D4I; -.
DR   PDBsum; 7D5S; -.
DR   PDBsum; 7D5T; -.
DR   PDBsum; 7D63; -.
DR   PDBsum; 7SUK; -.
DR   AlphaFoldDB; P39990; -.
DR   BMRB; P39990; -.
DR   EMDB; EMD-0949; -.
DR   EMDB; EMD-0950; -.
DR   EMDB; EMD-0951; -.
DR   EMDB; EMD-0952; -.
DR   EMDB; EMD-0953; -.
DR   EMDB; EMD-0954; -.
DR   EMDB; EMD-0955; -.
DR   EMDB; EMD-11357; -.
DR   EMDB; EMD-11358; -.
DR   EMDB; EMD-11359; -.
DR   EMDB; EMD-11360; -.
DR   EMDB; EMD-11361; -.
DR   EMDB; EMD-11807; -.
DR   EMDB; EMD-11808; -.
DR   EMDB; EMD-30574; -.
DR   EMDB; EMD-30584; -.
DR   EMDB; EMD-30585; -.
DR   EMDB; EMD-30588; -.
DR   EMDB; EMD-3683; -.
DR   EMDB; EMD-6695; -.
DR   EMDB; EMD-6696; -.
DR   EMDB; EMD-6972; -.
DR   EMDB; EMD-6974; -.
DR   EMDB; EMD-8012; -.
DR   EMDB; EMD-8014; -.
DR   EMDB; EMD-8473; -.
DR   EMDB; EMD-9964; -.
DR   SMR; P39990; -.
DR   BioGRID; 36703; 217.
DR   ComplexPortal; CPX-1604; Small ribosomal subunit processome.
DR   ComplexPortal; CPX-25; U4/U6.U5 tri-small nuclear ribonucleoprotein complex.
DR   ComplexPortal; CPX-31; U4 small nuclear ribonucleoprotein complex.
DR   ComplexPortal; CPX-32; U4/U6 small nuclear ribonucleoprotein complex.
DR   ComplexPortal; CPX-729; Box C/D snoRNP complex.
DR   DIP; DIP-2870N; -.
DR   IntAct; P39990; 31.
DR   MINT; P39990; -.
DR   STRING; 4932.YEL026W; -.
DR   iPTMnet; P39990; -.
DR   MaxQB; P39990; -.
DR   PaxDb; 4932-YEL026W; -.
DR   PeptideAtlas; P39990; -.
DR   EnsemblFungi; YEL026W_mRNA; YEL026W; YEL026W.
DR   GeneID; 856687; -.
DR   KEGG; sce:YEL026W; -.
DR   AGR; SGD:S000000752; -.
DR   SGD; S000000752; SNU13.
DR   VEuPathDB; FungiDB:YEL026W; -.
DR   eggNOG; KOG3387; Eukaryota.
DR   GeneTree; ENSGT00550000074840; -.
DR   HOGENOM; CLU_084513_4_1_1; -.
DR   InParanoid; P39990; -.
DR   OMA; IKNQIYA; -.
DR   OrthoDB; 5481533at2759; -.
DR   BioCyc; YEAST:G3O-30149-MONOMER; -.
DR   Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   BioGRID-ORCS; 856687; 2 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P39990; -.
DR   PRO; PR:P39990; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P39990; Protein.
DR   GO; GO:0031428; C:box C/D RNP complex; IDA:SGD.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; NAS:ComplexPortal.
DR   GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR   GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR   GO; GO:0005681; C:spliceosomal complex; NAS:ComplexPortal.
DR   GO; GO:0005687; C:U4 snRNP; NAS:ComplexPortal.
DR   GO; GO:0071001; C:U4/U6 snRNP; NAS:ComplexPortal.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:SGD.
DR   GO; GO:0003723; F:RNA binding; IMP:SGD.
DR   GO; GO:0034511; F:U3 snoRNA binding; IDA:GO_Central.
DR   GO; GO:0030621; F:U4 snRNA binding; IDA:SGD.
DR   GO; GO:0000494; P:box C/D RNA 3'-end processing; IDA:ComplexPortal.
DR   GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR   GO; GO:1905216; P:positive regulation of RNA binding; IDA:SGD.
DR   GO; GO:0000452; P:snoRNA guided rRNA 2'-O-methylation; IDA:ComplexPortal.
DR   GO; GO:0000245; P:spliceosomal complex assembly; NAS:ComplexPortal.
DR   CDD; cd21104; SNU13; 1.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   InterPro; IPR002415; H/ACA_rnp_Nhp2-like.
DR   InterPro; IPR029064; Ribosomal_eL30-like_sf.
DR   InterPro; IPR004037; Ribosomal_eL8-like_CS.
DR   InterPro; IPR004038; Ribosomal_eL8/eL30/eS12/Gad45.
DR   InterPro; IPR018492; Ribosomal_eL8/Nhp2.
DR   PANTHER; PTHR23105:SF38; NHP2-LIKE PROTEIN 1; 1.
DR   PANTHER; PTHR23105; RIBOSOMAL PROTEIN L7AE FAMILY MEMBER; 1.
DR   Pfam; PF01248; Ribosomal_L7Ae; 1.
DR   PRINTS; PR00881; L7ARS6FAMILY.
DR   PRINTS; PR00883; NUCLEARHMG.
DR   SUPFAM; SSF55315; L30e-like; 1.
DR   PROSITE; PS01082; RIBOSOMAL_L7AE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW   Ribonucleoprotein; Ribosome biogenesis; RNA-binding; rRNA processing;
KW   Spliceosome.
FT   CHAIN           1..126
FT                   /note="13 kDa ribonucleoprotein-associated protein"
FT                   /id="PRO_0000136777"
FT   MUTAGEN         59
FT                   /note="E->A: Impairs binding to U4 snRNA, but not U3
FT                   snoRNA. Causes pre-mRNA splicing and pre-rRNA processing
FT                   defects."
FT                   /evidence="ECO:0000269|PubMed:14730029"
FT   MUTAGEN         81
FT                   /note="V->L: Impairs binding to U4 snRNA, but not U3
FT                   snoRNA, and causes pre rRNA processing defects and an
FT                   accumulation of unspliced U3 snoRNA; when associated with
FT                   A-84."
FT                   /evidence="ECO:0000269|PubMed:14730029"
FT   MUTAGEN         84
FT                   /note="R->A: Impairs binding to U4 snRNA, but not U3
FT                   snoRNA, and causes pre rRNA processing defects and an
FT                   accumulation of unspliced U3 snoRNA; when associated with
FT                   L-81."
FT                   /evidence="ECO:0000269|PubMed:14730029"
FT   HELIX           14..29
FT                   /evidence="ECO:0007829|PDB:4NUT"
FT   STRAND          33..36
FT                   /evidence="ECO:0007829|PDB:4NUT"
FT   HELIX           37..46
FT                   /evidence="ECO:0007829|PDB:4NUT"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:4NUT"
FT   HELIX           61..64
FT                   /evidence="ECO:0007829|PDB:4NUT"
FT   HELIX           66..74
FT                   /evidence="ECO:0007829|PDB:4NUT"
FT   STRAND          78..82
FT                   /evidence="ECO:0007829|PDB:4NUT"
FT   HELIX           84..90
FT                   /evidence="ECO:0007829|PDB:4NUT"
FT   STRAND          98..103
FT                   /evidence="ECO:0007829|PDB:4NUT"
FT   HELIX           110..124
FT                   /evidence="ECO:0007829|PDB:4NUT"
SQ   SEQUENCE   126 AA;  13569 MW;  4489780153E8F182 CRC64;
     MSAPNPKAFP LADAALTQQI LDVVQQAANL RQLKKGANEA TKTLNRGISE FIIMAADCEP
     IEILLHLPLL CEDKNVPYVF VPSRVALGRA CGVSRPVIAA SITTNDASAI KTQIYAVKDK
     IETLLI
//