ISY1_YEAST
ID ISY1_YEAST Reviewed; 235 AA.
AC P21374; D6VWM1;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Pre-mRNA-splicing factor ISY1;
DE AltName: Full=Interactor of SYF1;
DE AltName: Full=PRP19-associated complex protein 30;
GN Name=ISY1; Synonyms=NTC30, UTR3; OrderedLocusNames=YJR050W; ORFNames=J1657;
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 PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2158927; DOI=10.1016/0378-1119(90)90297-5;
RA Melnick L., Sherman F.;
RT "Nucleotide sequence of the COR region: a cluster of six genes in the yeast
RT Saccharomyces cerevisiae.";
RL Gene 87:157-166(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7975898; DOI=10.1002/yea.320100611;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Revised nucleotide sequence of the COR region of yeast Saccharomyces
RT cerevisiae chromosome X.";
RL Yeast 10:811-818(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 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 [6]
RP FUNCTION, INTERACTION WITH SYF1, AND IDENTIFICATION IN THE PRP19-ASSOCIATED
RP COMPLEX.
RX PubMed=10094305; DOI=10.1017/s1355838299981396;
RA Dix I., Russell C.S., Yehuda S.B., Kupiec M., Beggs J.D.;
RT "The identification and characterization of a novel splicing protein,
RT Isy1p, of Saccharomyces cerevisiae.";
RL RNA 5:360-368(1999).
RN [7]
RP INTERACTION WITH CEF1; CLF1 AND SYF1.
RX PubMed=11102353; DOI=10.1093/genetics/156.4.1503;
RA Ben-Yehuda S., Dix I., Russell C.S., McGarvey M., Beggs J.D., Kupiec M.;
RT "Genetic and physical interactions between factors involved in both cell
RT cycle progression and pre-mRNA splicing in Saccharomyces cerevisiae.";
RL Genetics 156:1503-1517(2000).
RN [8]
RP FUNCTION, INTERACTION WITH CEF1, AND IDENTIFICATION IN THE SPLICEOSOME.
RX PubMed=11018040; DOI=10.1074/jbc.m006958200;
RA Chen C.-H., Tsai W.-Y., Chen H.-R., Wang C.-H., Cheng S.-C.;
RT "Identification and characterization of two novel components of the Prp19p-
RT associated complex, Ntc30p and Ntc20p.";
RL J. Biol. Chem. 276:488-494(2001).
RN [9]
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 [10]
RP IDENTIFICATION IN THE PRP19-ASSOCIATED COMPLEX.
RX PubMed=11842115; DOI=10.1093/nar/30.4.1029;
RA Chen C.-H., Yu W.-C., Tsao T.Y., Wang L.-Y., Chen H.-R., Lin J.-Y.,
RA Tsai W.-Y., Cheng S.-C.;
RT "Functional and physical interactions between components of the Prp19p-
RT associated complex.";
RL Nucleic Acids Res. 30:1029-1037(2002).
RN [11]
RP FUNCTION.
RX PubMed=12384582; DOI=10.1093/nar/gkf563;
RA Dahan O., Kupiec M.;
RT "Mutations in genes of Saccharomyces cerevisiae encoding pre-mRNA splicing
RT factors cause cell cycle arrest through activation of the spindle
RT checkpoint.";
RL Nucleic Acids Res. 30:4361-4370(2002).
RN [12]
RP INTERACTION WITH CLF1; CWC2 AND SYF1.
RX PubMed=12088152; DOI=10.1017/s1355838202025050;
RA Ohi M.D., Gould K.L.;
RT "Characterization of interactions among the Cef1p-Prp19p-associated
RT splicing complex.";
RL RNA 8:798-815(2002).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [14]
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 [15]
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 pre-mRNA splicing and cell cycle control. As a
CC component of the NTC complex (or PRP19-associated complex), associates
CC to the spliceosome to mediate conformational rearrangement or to
CC stabilize the structure of the spliceosome after U4 snRNA dissociation,
CC which leads to spliceosome maturation. The cell cycle arrest of SYF2
CC defective cells may be due to the inefficient splicing of TUB1. Also
CC involved in DNA repair. {ECO:0000269|PubMed:10094305,
CC ECO:0000269|PubMed:11018040, ECO:0000269|PubMed:12384582}.
CC -!- SUBUNIT: Belongs to the NTC complex (or PRP19-associated complex),
CC composed of at least CEF1, CLF1, ISY1, NTC20, SNT309, SYF1, SYF2, and
CC PRP19. The NTC complex associates with the spliceosome after the
CC release of the U1 and U4 snRNAs and forms the CWC spliceosome
CC subcomplex (or CEF1-associated complex) reminiscent of a late-stage
CC spliceosome composed also of the U2, U5 and U6 snRNAs and at least
CC BUD13, BUD31, BRR2, CDC40, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23,
CC CWC24, CWC25, CWC27, ECM2, HSH155, IST3, LEA1, MSL1, PRP8, PRP9, PRP11,
CC PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3,
CC SNU114, SPP2, RSE1 and YJU2. Interacts with CEF1, CWC2, CLF1, and SYF1.
CC {ECO:0000269|PubMed:10094305, ECO:0000269|PubMed:11018040,
CC ECO:0000269|PubMed:11102353, ECO:0000269|PubMed:11842115,
CC ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:12088152}.
CC -!- INTERACTION:
CC P21374; Q12309: CLF1; NbExp=4; IntAct=EBI-9382, EBI-484;
CC P21374; P32523: PRP19; NbExp=6; IntAct=EBI-9382, EBI-493;
CC P21374; Q04048: SYF1; NbExp=4; IntAct=EBI-9382, EBI-540;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1990 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ISY1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB59345.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M37696; AAB59345.1; ALT_INIT; Genomic_DNA.
DR EMBL; L26347; AAA62858.1; -; Genomic_DNA.
DR EMBL; L36344; AAA88753.1; -; Genomic_DNA.
DR EMBL; Z49550; CAA89578.1; -; Genomic_DNA.
DR EMBL; AY558078; AAS56404.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08837.1; -; Genomic_DNA.
DR PIR; S46590; S46590.
DR RefSeq; NP_012584.3; NM_001181708.3.
DR PDB; 5GMK; EM; 3.40 A; H=1-235.
DR PDB; 5LJ3; EM; 3.80 A; G=1-235.
DR PDB; 5LJ5; EM; 3.80 A; G=1-235.
DR PDB; 6J6G; EM; 3.20 A; H=1-235.
DR PDB; 6J6H; EM; 3.60 A; H=1-235.
DR PDB; 6J6N; EM; 3.86 A; H=1-235.
DR PDB; 6J6Q; EM; 3.70 A; H=1-235.
DR PDBsum; 5GMK; -.
DR PDBsum; 5LJ3; -.
DR PDBsum; 5LJ5; -.
DR PDBsum; 6J6G; -.
DR PDBsum; 6J6H; -.
DR PDBsum; 6J6N; -.
DR PDBsum; 6J6Q; -.
DR AlphaFoldDB; P21374; -.
DR SMR; P21374; -.
DR BioGRID; 33803; 194.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR ComplexPortal; CPX-1885; NineTeen complex.
DR DIP; DIP-1682N; -.
DR IntAct; P21374; 15.
DR MINT; P21374; -.
DR STRING; 4932.YJR050W; -.
DR iPTMnet; P21374; -.
DR MaxQB; P21374; -.
DR PaxDb; P21374; -.
DR PRIDE; P21374; -.
DR EnsemblFungi; YJR050W_mRNA; YJR050W; YJR050W.
DR GeneID; 853509; -.
DR KEGG; sce:YJR050W; -.
DR SGD; S000003811; ISY1.
DR VEuPathDB; FungiDB:YJR050W; -.
DR eggNOG; KOG3068; Eukaryota.
DR GeneTree; ENSGT00390000014109; -.
DR HOGENOM; CLU_043453_2_1_1; -.
DR InParanoid; P21374; -.
DR OMA; QWHIDHT; -.
DR BioCyc; YEAST:G3O-31685-MON; -.
DR Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR PRO; PR:P21374; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P21374; protein.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:SGD.
DR GO; GO:0071020; C:post-spliceosomal complex; IDA:SGD.
DR GO; GO:0000974; C:Prp19 complex; IDA:SGD.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IDA:SGD.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:SGD.
DR GO; GO:0000350; P:generation of catalytic spliceosome for second transesterification step; IMP:SGD.
DR GO; GO:0000389; P:mRNA 3'-splice site recognition; IMP:SGD.
DR DisProt; DP01593; -.
DR Gene3D; 1.10.287.660; -; 1.
DR InterPro; IPR029012; Helix_hairpin_bin_sf.
DR InterPro; IPR009360; Isy1.
DR InterPro; IPR037200; Isy1_sf.
DR PANTHER; PTHR13021; PTHR13021; 1.
DR Pfam; PF06246; Isy1; 1.
DR SUPFAM; SSF140102; SSF140102; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Spliceosome.
FT CHAIN 1..235
FT /note="Pre-mRNA-splicing factor ISY1"
FT /id="PRO_0000192976"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:5GMK"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 45..63
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 72..95
FT /evidence="ECO:0007829|PDB:6J6G"
SQ SEQUENCE 235 AA; 28024 MW; F88D74C247CF590C CRC64;
MSRNVDKANS VLVRFQEQQA ESAGGYKDYS RYQRPRNVSK VKSIKEANEW KRQVSKEIKQ
KSTRIYDPSL NEMQIAELND ELNNLFKEWK RWQWHIDHTL MEKKTKRKRL EDSHVLMNSG
KLINGKRYFG RALELPEVKE WLKQSQRQND GGSINTKCIP KDRNDFYYHG KVTAALTEFE
ANWTSILKAH YNVPVNEDEE EMSRQTQEIH VPTLADMEHW LVQRRKKKLM DELNL
