CUS1_YEAST
ID CUS1_YEAST Reviewed; 436 AA.
AC Q02554; D6W066; Q04012;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Cold sensitive U2 snRNA suppressor 1;
GN Name=CUS1; OrderedLocusNames=YMR240C; ORFNames=YM9408.02C;
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].
RX PubMed=8566755; DOI=10.1101/gad.10.2.220;
RA Wells S.E., Neville M., Haynes M., Wang J., Igel H., Ares M. Jr.;
RT "CUS1, a suppressor of cold-sensitive U2 snRNA mutations, is a novel yeast
RT splicing factor homologous to human SAP 145.";
RL Genes Dev. 10:220-232(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 IDENTIFICATION IN THE CWC COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11884590; DOI=10.1128/mcb.22.7.2011-2024.2002;
RA Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
RT "Proteomics analysis reveals stable multiprotein complexes in both fission
RT and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT splicing factors, and snRNAs.";
RL Mol. Cell. Biol. 22:2011-2024(2002).
RN [6]
RP INTERACTION WITH RDS3.
RX PubMed=14517302; DOI=10.1128/mcb.23.20.7339-7349.2003;
RA Wang Q., Rymond B.C.;
RT "Rds3p is required for stable U2 snRNP recruitment to the splicing
RT apparatus.";
RL Mol. Cell. Biol. 23:7339-7349(2003).
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 THR-104; THR-112 AND SER-114, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Essential splicing protein required for U2 snRNP binding to
CC pre-mRNA during spliceosome assembly.
CC -!- SUBUNIT: Belongs to the CWC complex (or CEF1-associated complex), a
CC spliceosome sub-complex reminiscent of a late-stage spliceosome
CC composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2,
CC CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24,
CC CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9,
CC PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3,
CC SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts
CC with RDS3. {ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:14517302}.
CC -!- INTERACTION:
CC Q02554; Q99181: HSH49; NbExp=6; IntAct=EBI-654, EBI-8579;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 1830 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: To mammalian SAP 145. Some, to C.elegans ZK632.11.
CC {ECO:0000305}.
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DR EMBL; U27016; AAB04171.1; -; Genomic_DNA.
DR EMBL; Z48756; CAA88650.1; -; Genomic_DNA.
DR EMBL; AY723856; AAU09773.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10140.1; -; Genomic_DNA.
DR PIR; S56054; S56054.
DR RefSeq; NP_013967.1; NM_001182747.1.
DR PDB; 5GM6; EM; 3.50 A; H=1-436.
DR PDB; 5LSB; X-ray; 2.70 A; B/D/H=290-368.
DR PDB; 5LSL; X-ray; 1.65 A; E/F/G/H=290-368.
DR PDB; 5NRL; EM; 7.20 A; Q=1-435.
DR PDB; 5ZWM; EM; 3.40 A; 2=1-436.
DR PDB; 5ZWO; EM; 3.90 A; 2=1-436.
DR PDB; 6G90; EM; 4.00 A; Q=1-435.
DR PDB; 7OQB; EM; 9.00 A; Q=1-436.
DR PDB; 7OQE; EM; 5.90 A; Q=1-436.
DR PDBsum; 5GM6; -.
DR PDBsum; 5LSB; -.
DR PDBsum; 5LSL; -.
DR PDBsum; 5NRL; -.
DR PDBsum; 5ZWM; -.
DR PDBsum; 5ZWO; -.
DR PDBsum; 6G90; -.
DR PDBsum; 7OQB; -.
DR PDBsum; 7OQE; -.
DR AlphaFoldDB; Q02554; -.
DR SMR; Q02554; -.
DR BioGRID; 35419; 242.
DR ComplexPortal; CPX-1647; SF3B complex.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR ComplexPortal; CPX-26; U2 small nuclear ribonucleoprotein complex.
DR DIP; DIP-910N; -.
DR IntAct; Q02554; 31.
DR MINT; Q02554; -.
DR STRING; 4932.YMR240C; -.
DR iPTMnet; Q02554; -.
DR MaxQB; Q02554; -.
DR PaxDb; Q02554; -.
DR PRIDE; Q02554; -.
DR TopDownProteomics; Q02554; -.
DR EnsemblFungi; YMR240C_mRNA; YMR240C; YMR240C.
DR GeneID; 855281; -.
DR KEGG; sce:YMR240C; -.
DR SGD; S000004853; CUS1.
DR VEuPathDB; FungiDB:YMR240C; -.
DR eggNOG; KOG2330; Eukaryota.
DR GeneTree; ENSGT00390000006734; -.
DR HOGENOM; CLU_014435_2_1_1; -.
DR InParanoid; Q02554; -.
DR OMA; IEWFDCD; -.
DR BioCyc; YEAST:G3O-32920-MON; -.
DR PRO; PR:Q02554; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q02554; protein.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0005686; C:U2 snRNP; IDA:SGD.
DR GO; GO:0071004; C:U2-type prespliceosome; IDA:SGD.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IPI:ComplexPortal.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IPI:SGD.
DR GO; GO:0000245; P:spliceosomal complex assembly; IDA:SGD.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR DisProt; DP01978; -.
DR InterPro; IPR007180; DUF382.
DR InterPro; IPR006568; PSP_pro-rich.
DR Pfam; PF04037; DUF382; 1.
DR Pfam; PF04046; PSP; 1.
DR SMART; SM00581; PSP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT CHAIN 1..436
FT /note="Cold sensitive U2 snRNA suppressor 1"
FT /id="PRO_0000079565"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 112
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT VARIANT 181
FT /note="E -> K (in allele CUS1-54; cold-sensitive growth
FT suppressor)"
FT HELIX 296..302
FT /evidence="ECO:0007829|PDB:5LSL"
FT HELIX 313..319
FT /evidence="ECO:0007829|PDB:5LSL"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:5LSL"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:5LSL"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:5LSL"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:5LSL"
SQ SEQUENCE 436 AA; 50253 MW; 0204B3A666AF7336 CRC64;
MARTKSRKRS GNNQNKNASV VNNKAEIAAM IDARRLEQKK KGGVTNSKGK TNKVVDAKLE
KEFKDVLQRF QVQENDTPKE ITKDEKNNHV VIVEKNPVMN RKHTAEDELE DTPSDGIEEH
LSARKRRKTE KPSLSQLKSQ VPYPQIIEWY DCDARYPGLL ASIKCTKNVI PVPSHWQSKK
EYLSGRSLLG KRPFELPDII KKTNIEQMRS TLPQSGLDGQ DEKSLKEASR ARVQPKMGAL
DLDYKKLHDV FFKIGANWKP DHLLCFGDVY YENRNLFEET NWKRMVDHKR PGRISQELRA
IMNLPEGQLP PWCMKMKDIG LPTGYPDLKI AGLNWDITNL KGDVYGKIIP NHHSRSKKQG
RNYFGALISF ETPEFENSKE DTQANAENGR QDDKIDDEVE HKLDHFQEDI SEVTSAEEKL
ERNEEESEKQ LYTVLK
