CUS2_YEAST
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 03-AUG-2022, entry version 161.
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;
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;
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 -!- 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; 46.
DR ComplexPortal; CPX-26; U2 small nuclear ribonucleoprotein complex.
DR DIP; DIP-2316N; -.
DR IntAct; P53830; 6.
DR MINT; P53830; -.
DR STRING; 4932.YNL286W; -.
DR iPTMnet; P53830; -.
DR MaxQB; P53830; -.
DR PaxDb; P53830; -.
DR PRIDE; P53830; -.
DR EnsemblFungi; YNL286W_mRNA; YNL286W; YNL286W.
DR GeneID; 855430; -.
DR KEGG; sce:YNL286W; -.
DR SGD; S000005230; CUS2.
DR VEuPathDB; FungiDB:YNL286W; -.
DR eggNOG; KOG1548; Eukaryota.
DR GeneTree; ENSGT00390000009902; -.
DR HOGENOM; CLU_026945_2_0_1; -.
DR InParanoid; P53830; -.
DR OMA; NKWAKVV; -.
DR BioCyc; YEAST:G3O-33276-MON; -.
DR PRO; PR:P53830; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53830; protein.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005681; C:spliceosomal complex; IC: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:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0030620; F:U2 snRNA binding; IDA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC: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 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; PTHR15608; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 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 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
