ID   CUS2_YEAST              Reviewed;         285 AA.
AC   P53830; D6W0Q7; E9P8U4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 177.
DE   RecName: Full=Cold sensitive U2 snRNA suppressor 2;
GN   Name=CUS2; OrderedLocusNames=YNL286W; ORFNames=N0549;
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=9169873; DOI=10.1038/387s093;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(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   FUNCTION, INTERACTION WITH PRP11, AND ASSOCIATION WITH U2.
RX   PubMed=9710584; DOI=10.1128/mcb.18.9.5000;
RA   Yan D., Perriman R., Igel H., Howe K.J., Neville M., Ares M. Jr.;
RT   "CUS2, a yeast homolog of human Tat-SF1, rescues function of misfolded U2
RT   through an unusual RNA recognition motif.";
RL   Mol. Cell. Biol. 18:5000-5009(1998).
RN   [5]
RP   FUNCTION.
RX   PubMed=10640279; DOI=10.1101/gad.14.1.97;
RA   Perriman R., Ares M. Jr.;
RT   "ATP can be dispensable for prespliceosome formation in yeast.";
RL   Genes Dev. 14:97-107(2000).
RN   [6]
RP   IDENTIFICATION IN THE U2 SNRNP, AND IDENTIFICATION 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   [7]
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [9]
RP   FUNCTION.
RX   PubMed=18082608; DOI=10.1016/j.molcel.2007.09.022;
RA   Xu Y.Z., Query C.C.;
RT   "Competition between the ATPase Prp5 and branch region-U2 snRNA pairing
RT   modulates the fidelity of spliceosome assembly.";
RL   Mol. Cell 28:838-849(2007).
CC   -!- FUNCTION: U2 snRNP protein which helps to refold U2 into a structure
CC       favorable for its binding to SF3b and SF3a prior to spliceosome
CC       assembly. Mediates functional interactions between U2 RNA and PRP5.
CC       Enforces ATP dependence during formation of the prespliceosome by
CC       brokering an interaction between PRP5 and the U2 snRNP that depends on
CC       correct U2 RNA structure. {ECO:0000269|PubMed:10640279,
CC       ECO:0000269|PubMed:18082608, ECO:0000269|PubMed:9710584}.
CC   -!- SUBUNIT: Interacts with PRP11. Associates with the U2 snRNA.
CC       {ECO:0000269|PubMed:11804584, ECO:0000269|PubMed:9710584}.
CC   -!- INTERACTION:
CC       P53830; P49955: HSH155; NbExp=3; IntAct=EBI-28299, EBI-664;
CC   -!- MISCELLANEOUS: Present with 1360 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the HTATSF1 family. {ECO:0000305}.
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DR   EMBL; Z71562; CAA96203.1; -; Genomic_DNA.
DR   EMBL; AY558016; AAS56342.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10273.1; -; Genomic_DNA.
DR   PIR; S63260; S63260.
DR   RefSeq; NP_014113.1; NM_001183124.1.
DR   AlphaFoldDB; P53830; -.
DR   SMR; P53830; -.
DR   BioGRID; 35551; 48.
DR   ComplexPortal; CPX-26; U2 small nuclear ribonucleoprotein complex.
DR   DIP; DIP-2316N; -.
DR   FunCoup; P53830; 158.
DR   IntAct; P53830; 9.
DR   MINT; P53830; -.
DR   STRING; 4932.YNL286W; -.
DR   iPTMnet; P53830; -.
DR   PaxDb; 4932-YNL286W; -.
DR   PeptideAtlas; P53830; -.
DR   EnsemblFungi; YNL286W_mRNA; YNL286W; YNL286W.
DR   GeneID; 855430; -.
DR   KEGG; sce:YNL286W; -.
DR   AGR; SGD:S000005230; -.
DR   SGD; S000005230; CUS2.
DR   VEuPathDB; FungiDB:YNL286W; -.
DR   eggNOG; KOG1548; Eukaryota.
DR   HOGENOM; CLU_026945_2_0_1; -.
DR   InParanoid; P53830; -.
DR   OMA; IVISKPM; -.
DR   OrthoDB; 10258585at2759; -.
DR   BioCyc; YEAST:G3O-33276-MONOMER; -.
DR   BioGRID-ORCS; 855430; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P53830; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53830; protein.
DR   GO; GO:0005634; C:nucleus; NAS:ComplexPortal.
DR   GO; GO:0005681; C:spliceosomal complex; NAS:ComplexPortal.
DR   GO; GO:0005686; C:U2 snRNP; IPI:SGD.
DR   GO; GO:0005684; C:U2-type spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0030620; F:U2 snRNA binding; IDA:GO_Central.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; NAS:ComplexPortal.
DR   GO; GO:0034337; P:RNA folding; IDA:SGD.
DR   GO; GO:1903241; P:U2-type prespliceosome assembly; IMP:GO_Central.
DR   CDD; cd12281; RRM1_TatSF1_like; 1.
DR   CDD; cd12285; RRM3_RBM39_like; 1.
DR   FunFam; 3.30.70.330:FF:001119; Cold sensitive u2 snRNA suppressor; 1.
DR   Gene3D; 3.30.70.330; -; 2.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR034393; TatSF1-like.
DR   InterPro; IPR034392; TatSF1-like_RRM1.
DR   PANTHER; PTHR15608:SF0; HIV TAT-SPECIFIC FACTOR 1; 1.
DR   PANTHER; PTHR15608; SPLICING FACTOR U2AF-ASSOCIATED PROTEIN 2; 1.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   mRNA processing; mRNA splicing; Phosphoprotein; Reference proteome; Repeat;
KW   RNA-binding; Spliceosome.
FT   CHAIN           1..285
FT                   /note="Cold sensitive U2 snRNA suppressor 2"
FT                   /id="PRO_0000082037"
FT   DOMAIN          45..130
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          183..265
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          135..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          265..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..285
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         163
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   CONFLICT        235
FT                   /note="F -> L (in Ref. 3; AAS56342)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   285 AA;  32284 MW;  69A926BF0DB2C6FE CRC64;
     MDADELELKG HLKKLKKEEL LRRKQLKESN LQKRELEYNN ASKNTSIYIS GLPTDKTTKE
     GLTEQFCKYG MIRTNRDGEP LCKLYVNDKG AFKGDALITY SKEESVTLAI EMMNESIFLG
     KQIRVERAQF QNKEGDNMHG KENDLKEFNG PEPPIKRLKK AKSEGEGEVI DYNDDESLAK
     ADRTVIFANV FNIYKSYTND DINDIQEDLL EGCEEIGQVD SISVSPNKGE ATVVFKNNKV
     ALQCCKIMTG RYFDGQKLLA FISGDENTSS TSDKNEDSEV EDDLI
//