SNU13_YEAST
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 03-AUG-2022, entry version 189.
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 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 AlphaFoldDB; P39990; -.
DR BMRB; P39990; -.
DR SMR; P39990; -.
DR BioGRID; 36703; 209.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
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; 30.
DR MINT; P39990; -.
DR STRING; 4932.YEL026W; -.
DR iPTMnet; P39990; -.
DR MaxQB; P39990; -.
DR PaxDb; P39990; -.
DR PRIDE; P39990; -.
DR EnsemblFungi; YEL026W_mRNA; YEL026W; YEL026W.
DR GeneID; 856687; -.
DR KEGG; sce:YEL026W; -.
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; KPFYVRF; -.
DR BioCyc; YEAST:G3O-30149-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
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:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IC: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; IC:ComplexPortal.
DR GO; GO:0005687; C:U4 snRNP; IC:ComplexPortal.
DR GO; GO:0071001; C:U4/U6 snRNP; IC: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:GO_Central.
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; IC:ComplexPortal.
DR Gene3D; 3.30.1330.30; -; 1.
DR InterPro; IPR002415; H/ACA_rnp_Nhp2-like.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR InterPro; IPR018492; Ribosomal_L7Ae/L8/Nhp2.
DR InterPro; IPR004037; Ribosomal_L7Ae_CS.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR PRINTS; PR00881; L7ARS6FAMILY.
DR PRINTS; PR00883; NUCLEARHMG.
DR SUPFAM; SSF55315; SSF55315; 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
