SNU66_YEAST
ID SNU66_YEAST Reviewed; 587 AA.
AC Q12420; D6W308;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=66 kDa U4/U6.U5 small nuclear ribonucleoprotein component;
GN Name=SNU66; OrderedLocusNames=YOR308C; ORFNames=05667;
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 96604 / S288c / FY1679;
RX PubMed=8896266;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1021::aid-yea981>3.0.co;2-7;
RA Pearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A.,
RA Schweizer M.;
RT "Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome
RT XV reveals regions of similarity to chromosomes I and XIII.";
RL Yeast 12:1021-1031(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9153758;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<479::aid-yea104>3.0.co;2-g;
RA Poirey R., Cziepluch C., Tobiasch E., Pujol A., Kordes E., Jauniaux J.-C.;
RT "Sequence and analysis of a 36.2 kb fragment from the right arm of yeast
RT chromosome XV reveals 19 open reading frames including SNF2 (5' end), CPA1,
RT SLY41, a putative transport ATPase, a putative ribosomal protein and an
RT SNF2 homologue.";
RL Yeast 13:479-482(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, INTERACTION WITH BRR2, AND SUBCELLULAR LOCATION.
RX PubMed=11290703; DOI=10.1093/genetics/157.4.1451;
RA van Nues R.W., Beggs J.D.;
RT "Functional contacts with a range of splicing proteins suggest a central
RT role for Brr2p in the dynamic control of the order of events in
RT spliceosomes of Saccharomyces cerevisiae.";
RL Genetics 157:1451-1467(2001).
RN [8]
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 [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
RP INTERACTION WITH HUB1.
RX PubMed=15620657; DOI=10.1016/j.cub.2004.11.058;
RA Wilkinson C.R.M., Dittmar G.A.G., Ohi M.D., Uetz P., Jones N., Finley D.;
RT "Ubiquitin-like protein Hub1 is required for pre-mRNA splicing and
RT localization of an essential splicing factor in fission yeast.";
RL Curr. Biol. 14:2283-2288(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY
RP 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).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the U4/U6.U5 tri-snRNP particle, one of the
CC building blocks of the spliceosome. Required for pre-mRNA splicing.
CC {ECO:0000269|PubMed:11290703}.
CC -!- SUBUNIT: Component of the U4/U6-U5 tri-snRNP complex composed of the
CC U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31,
CC PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3,
CC SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.
CC Interacts with the pre-mRNA-splicing helicase BRR2 and the ubiquitin-
CC like modifier HUB1. {ECO:0000269|PubMed:10377396,
CC ECO:0000269|PubMed:10449419, ECO:0000269|PubMed:11290703,
CC ECO:0000269|PubMed:11804584, ECO:0000269|PubMed:15620657}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11290703,
CC ECO:0000269|PubMed:14562095}.
CC -!- SIMILARITY: Belongs to the SNU66/SART1 family. {ECO:0000305}.
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DR EMBL; X90565; CAA62162.1; -; Genomic_DNA.
DR EMBL; Z75216; CAA99628.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11074.1; -; Genomic_DNA.
DR PIR; S58319; S58319.
DR RefSeq; NP_014953.3; NM_001183728.3.
DR PDB; 3PLU; X-ray; 1.40 A; C/D=6-24.
DR PDB; 3PLV; X-ray; 1.90 A; C=37-57.
DR PDB; 5GAN; EM; 3.60 A; E=540-560.
DR PDB; 5GAO; EM; 3.60 A; E=540-560.
DR PDB; 5NRL; EM; 7.20 A; E=1-587.
DR PDB; 5ZWM; EM; 3.40 A; O=1-587.
DR PDB; 5ZWO; EM; 3.90 A; O=1-587.
DR PDBsum; 3PLU; -.
DR PDBsum; 3PLV; -.
DR PDBsum; 5GAN; -.
DR PDBsum; 5GAO; -.
DR PDBsum; 5NRL; -.
DR PDBsum; 5ZWM; -.
DR PDBsum; 5ZWO; -.
DR AlphaFoldDB; Q12420; -.
DR SMR; Q12420; -.
DR BioGRID; 34697; 266.
DR ComplexPortal; CPX-25; U4/U6.U5 tri-small nuclear ribonucleoprotein complex.
DR DIP; DIP-5216N; -.
DR IntAct; Q12420; 21.
DR MINT; Q12420; -.
DR STRING; 4932.YOR308C; -.
DR iPTMnet; Q12420; -.
DR MaxQB; Q12420; -.
DR PaxDb; Q12420; -.
DR PRIDE; Q12420; -.
DR EnsemblFungi; YOR308C_mRNA; YOR308C; YOR308C.
DR GeneID; 854485; -.
DR KEGG; sce:YOR308C; -.
DR SGD; S000005835; SNU66.
DR VEuPathDB; FungiDB:YOR308C; -.
DR eggNOG; KOG2217; Eukaryota.
DR HOGENOM; CLU_018358_0_0_1; -.
DR InParanoid; Q12420; -.
DR OMA; FNGRHYR; -.
DR BioCyc; YEAST:G3O-33792-MON; -.
DR PRO; PR:Q12420; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12420; protein.
DR GO; GO:0005634; C:nucleus; IDA:CACAO.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:SGD.
DR GO; GO:0000481; P:maturation of 5S rRNA; IMP:SGD.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR InterPro; IPR045347; HIND.
DR InterPro; IPR005011; SNU66/SART1.
DR PANTHER; PTHR14152; PTHR14152; 2.
DR Pfam; PF19252; HIND; 2.
DR Pfam; PF03343; SART-1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Spliceosome.
FT CHAIN 1..587
FT /note="66 kDa U4/U6.U5 small nuclear ribonucleoprotein
FT component"
FT /id="PRO_0000232635"
FT REGION 403..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..568
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT HELIX 9..18
FT /evidence="ECO:0007829|PDB:3PLU"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:3PLV"
SQ SEQUENCE 587 AA; 66430 MW; 154BC3873DD6B0FA CRC64;
MNKTENLSIE ETNEIREKLG MKPIPVFQEK NTDHKESLSI EETNELRASL GLKLIPPQQN
FNSSPPNVHN TSKIDELREK ITKFQKKANA PLRMAHLLEE TNVNDDSSWL ENMDAIPSSH
ESKRSSTLPR KGATKEDENI DLHNVQVSYN IEALSPKKDT ILTLKESSIF DDTDSTEVLE
NVKAAEENAD REKLRLRQMN KDRRQKKKIL NVSSLDIEEE EEGEKHSITT THLIIGAEQG
VMKAPNTISA KPPTGKVKVN FDSANNMSDE DGGDFKPLKI KKRKIKDPRS TKARKSKITD
KMEIVKLVDE DESLSWMEEE QPVTIINPRT SSNNELKGPE DLAREIEKAR DEEKRRTESI
LKMREISNSI VVDEKVTFLN TLDTSLSERS ATENKVKVHG EGEKNIGDVT NGHTKEGSGN
NTLTEAVNNE PNYEGDAENA PNFFSGLAST LGYLRKKSVF TTGDVDLKPG KDVNNSESLR
RDVRNKEHTG TGTYTKDKLH GLEQFTSSDS SNANTHSKRQ DHYDPDIKLV YRDEKGNRLT
TKEAYKKLSQ KFHGTKSNKK KRAKMKSRIE ARKNTPENGS LFEFDDN
