RU17_YEAST
ID RU17_YEAST Reviewed; 300 AA.
AC Q00916; D6VVM3;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=U1 small nuclear ribonucleoprotein 70 kDa homolog;
DE Short=U1 70K;
DE Short=U1 snRNP 70 kDa homolog;
DE Short=U1-70K;
DE AltName: Full=U1 small nuclear ribonucleoprotein SNP1;
DE Short=U1 snRNP protein SNP1;
GN Name=SNP1; OrderedLocusNames=YIL061C;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=1714384; DOI=10.1002/j.1460-2075.1991.tb07805.x;
RA Smith V., Barrell B.G.;
RT "Cloning of a yeast U1 snRNP 70K protein homologue: functional conservation
RT of an RNA-binding domain between humans and yeast.";
RL EMBO J. 10:2627-2634(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
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 [4]
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 [5]
RP U1 RNA-BINDING.
RX PubMed=1387202; DOI=10.1093/nar/20.15.4009;
RA Kao H.-Y., Siliciano P.G.;
RT "The yeast homolog of the U1 snRNP protein 70K is encoded by the SNP1
RT gene.";
RL Nucleic Acids Res. 20:4009-4013(1992).
RN [6]
RP MUTAGENESIS OF 18-PRO--PRO-98; 92-TRP--ALA-248; LYS-148; TYR-150 AND
RP PHE-152.
RX PubMed=7565787; DOI=10.1128/mcb.15.11.6341;
RA Hilleren P.J., Kao H.-Y., Siliciano P.G.;
RT "The amino-terminal domain of yeast U1-70K is necessary and sufficient for
RT function.";
RL Mol. Cell. Biol. 15:6341-6350(1995).
RN [7]
RP MUTAGENESIS OF 18-PRO--ASN-93; 92-TRP--ALA-248; LYS-148; TYR-150 AND
RP PHE-152.
RX PubMed=8643384;
RA Hilleren P.J., Kao H.-Y., Siliciano P.G.;
RT "The RRM domain is dispensable for yeast U1-70K function.";
RL Nucleic Acids Symp. Ser. 33:244-247(1995).
RN [8]
RP IDENTIFICATION IN U1 SNRNP BY MASS SPECTROMETRY.
RX PubMed=9012791; DOI=10.1073/pnas.94.2.385;
RA Neubauer G., Gottschalk A., Fabrizio P., Seraphin B., Luehrmann R.,
RA Mann M.;
RT "Identification of the proteins of the yeast U1 small nuclear
RT ribonucleoprotein complex by mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:385-390(1997).
RN [9]
RP IDENTIFICATION IN U1 SNRNP BY MASS SPECTROMETRY.
RX PubMed=9630245;
RA Gottschalk A., Tang J., Puig O., Salgado J., Neubauer G., Colot H.V.,
RA Mann M., Seraphin B., Rosbash M., Luehrmann R., Fabrizio P.;
RT "A comprehensive biochemical and genetic analysis of the yeast U1 snRNP
RT reveals five novel proteins.";
RL RNA 4:374-393(1998).
RN [10]
RP INTERACTION WITH MRNA.
RX PubMed=10072386; DOI=10.1101/gad.13.5.581;
RA Zhang D., Rosbash M.;
RT "Identification of eight proteins that cross-link to pre-mRNA in the yeast
RT commitment complex.";
RL Genes Dev. 13:581-592(1999).
RN [11]
RP INTERACTION WITH EXO84 AND PRP8.
RX PubMed=11425851; DOI=10.1074/jbc.m100022200;
RA Awasthi S., Palmer R., Castro M., Mobarak C.D., Ruby S.W.;
RT "New roles for the Snp1 and Exo84 proteins in yeast pre-mRNA splicing.";
RL J. Biol. Chem. 276:31004-31015(2001).
RN [12]
RP IDENTIFICATION IN U1.U2.U4/U6.U5 PENTA-SNRNP COMPLEX BY 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 [13]
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).
CC -!- FUNCTION: Involved in nuclear mRNA splicing.
CC -!- SUBUNIT: Component of the spliceosome, where it is associated with
CC snRNP U1. Binds stem loop I of U1 snRNA. Interacts with mRNA.
CC {ECO:0000269|PubMed:10072386, ECO:0000269|PubMed:11425851,
CC ECO:0000269|PubMed:11804584, ECO:0000269|PubMed:9012791,
CC ECO:0000269|PubMed:9630245}.
CC -!- INTERACTION:
CC Q00916; P38261: EXO84; NbExp=2; IntAct=EBI-724, EBI-21567;
CC Q00916; P33334: PRP8; NbExp=3; IntAct=EBI-724, EBI-465;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 736 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z38060; CAA86162.1; -; Genomic_DNA.
DR EMBL; X59986; CAA42602.1; -; Genomic_DNA.
DR EMBL; AY558085; AAS56411.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08489.1; -; Genomic_DNA.
DR PIR; S16815; S16815.
DR RefSeq; NP_012203.1; NM_001179411.1.
DR PDB; 5ZWN; EM; 3.30 A; Q=1-300.
DR PDB; 6G90; EM; 4.00 A; B=1-300.
DR PDB; 6N7P; EM; 3.60 A; A=1-300.
DR PDB; 6N7R; EM; 3.20 A; A=1-300.
DR PDB; 6N7X; EM; 3.60 A; A=1-300.
DR PDB; 7OQC; EM; 4.10 A; B=1-300.
DR PDB; 7OQE; EM; 5.90 A; B=1-300.
DR PDBsum; 5ZWN; -.
DR PDBsum; 6G90; -.
DR PDBsum; 6N7P; -.
DR PDBsum; 6N7R; -.
DR PDBsum; 6N7X; -.
DR PDBsum; 7OQC; -.
DR PDBsum; 7OQE; -.
DR AlphaFoldDB; Q00916; -.
DR SMR; Q00916; -.
DR BioGRID; 34931; 91.
DR ComplexPortal; CPX-23; U1 small nuclear ribonucleoprotein complex.
DR DIP; DIP-663N; -.
DR IntAct; Q00916; 45.
DR MINT; Q00916; -.
DR STRING; 4932.YIL061C; -.
DR iPTMnet; Q00916; -.
DR MaxQB; Q00916; -.
DR PaxDb; Q00916; -.
DR PRIDE; Q00916; -.
DR EnsemblFungi; YIL061C_mRNA; YIL061C; YIL061C.
DR GeneID; 854749; -.
DR KEGG; sce:YIL061C; -.
DR SGD; S000001323; SNP1.
DR VEuPathDB; FungiDB:YIL061C; -.
DR eggNOG; KOG0113; Eukaryota.
DR GeneTree; ENSGT00940000160292; -.
DR HOGENOM; CLU_045151_4_1_1; -.
DR InParanoid; Q00916; -.
DR OMA; QEQANYK; -.
DR BioCyc; YEAST:G3O-31329-MON; -.
DR PRO; PR:Q00916; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; Q00916; protein.
DR GO; GO:0000243; C:commitment complex; IPI:SGD.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0005685; C:U1 snRNP; IDA:SGD.
DR GO; GO:0071004; C:U2-type prespliceosome; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IPI:SGD.
DR GO; GO:0017069; F:snRNA binding; IBA:GO_Central.
DR GO; GO:0030619; F:U1 snRNA binding; IPI:SGD.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; IC:ComplexPortal.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IPI:SGD.
DR CDD; cd12236; RRM_snRNP70; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034143; snRNP70_RRM.
DR InterPro; IPR022023; U1snRNP70_N.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF12220; U1snRNP70_N; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..300
FT /note="U1 small nuclear ribonucleoprotein 70 kDa homolog"
FT /id="PRO_0000081886"
FT DOMAIN 107..198
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 204..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 18..98
FT /note="Missing: Severely temperature-sensitive. Defective
FT in pre-mRNA splicing."
FT /evidence="ECO:0000269|PubMed:7565787"
FT MUTAGEN 18..93
FT /note="Missing: Fails to complement the growth and splicing
FT defective, temperature-sensitive phenotype of the null
FT allele at 30 degrees Celsius. No association with U1
FT snRNP."
FT /evidence="ECO:0000269|PubMed:8643384"
FT MUTAGEN 92..248
FT /note="Missing: Associates with U1 snRNP."
FT /evidence="ECO:0000269|PubMed:7565787,
FT ECO:0000269|PubMed:8643384"
FT MUTAGEN 148
FT /note="K->L: No splicing defects. Associates with U1 snRNP;
FT when associated with T-150 and L-152."
FT /evidence="ECO:0000269|PubMed:7565787,
FT ECO:0000269|PubMed:8643384"
FT MUTAGEN 150
FT /note="Y->T: No splicing defects. Associates with U1 snRNP;
FT when associated with L-148 and L-152."
FT /evidence="ECO:0000269|PubMed:7565787,
FT ECO:0000269|PubMed:8643384"
FT MUTAGEN 152
FT /note="F->L: No splicing defects. Associates with U1 snRNP;
FT when associated with L-148 and T-150."
FT /evidence="ECO:0000269|PubMed:7565787,
FT ECO:0000269|PubMed:8643384"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 10..15
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 45..58
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 66..90
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:5ZWN"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 147..156
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 158..170
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 177..185
FT /evidence="ECO:0007829|PDB:6N7R"
SQ SEQUENCE 300 AA; 34447 MW; 7D9E47BE66FE1EB8 CRC64;
MNYNLSKYPD DVSRLFKPRP PLSYKRPTDY PYAKRQTNPN ITGVANLLST SLKHYMEEFP
EGSPNNHLQR YEDIKLSKIK NAQLLDRRLQ NWNPNVDPHI KDTDPYRTIF IGRLPYDLDE
IELQKYFVKF GEIEKIRIVK DKITQKSKGY AFIVFKDPIS SKMAFKEIGV HRGIQIKDRI
CIVDIERGRT VKYFKPRRLG GGLGGRGYSN RDSRLPGRFA SASTSNPAER NYAPRLPRRE
TSSSAYSADR YGSSTLDARY RGNRPLLSAA TPTAAVTSVY KSRNSRTRES QPAPKEAPDY
