ID   SYF2_YEAST              Reviewed;         215 AA.
AC   P53277; D6VUR1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Pre-mRNA-splicing factor SYF2;
DE   AltName: Full=PRP19 complex protein 31;
DE   AltName: Full=Synthetic lethal with CDC40 protein 2;
GN   Name=SYF2; Synonyms=NTC31; OrderedLocusNames=YGR129W;
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=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(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, AND 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   [5]
RP   FUNCTION, AND IDENTIFICATION IN THE SPLICEOSOME.
RX   PubMed=11105756; DOI=10.1017/s1355838200000984;
RA   Russell C.S., Ben-Yehuda S., Dix I., Kupiec M., Beggs J.D.;
RT   "Functional analyses of interacting factors involved in both pre-mRNA
RT   splicing and cell cycle progression in Saccharomyces cerevisiae.";
RL   RNA 6:1565-1572(2000).
RN   [6]
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   [7]
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   [8]
RP   FUNCTION, AND GENETIC INTERACTION WITH ISY1.
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   [9]
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   [10]
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   [11]
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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-125, AND
RP   IDENTIFICATION BY 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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-124 AND SER-125, AND
RP   IDENTIFICATION BY 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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-125, 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: 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.
CC       {ECO:0000269|PubMed:11102353, ECO:0000269|PubMed:11105756,
CC       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, CLF1 and SYF1.
CC       {ECO:0000269|PubMed:11102353, ECO:0000269|PubMed:11105756,
CC       ECO:0000269|PubMed:11842115, ECO:0000269|PubMed:11884590}.
CC   -!- INTERACTION:
CC       P53277; Q03654: CEF1; NbExp=3; IntAct=EBI-23308, EBI-476;
CC       P53277; Q12309: CLF1; NbExp=2; IntAct=EBI-23308, EBI-484;
CC       P53277; P38302: NTC20; NbExp=2; IntAct=EBI-23308, EBI-20921;
CC       P53277; P32523: PRP19; NbExp=4; IntAct=EBI-23308, EBI-493;
CC       P53277; Q04048: SYF1; NbExp=3; IntAct=EBI-23308, EBI-540;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 1670 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SYF2 family. {ECO:0000305}.
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DR   EMBL; Z72914; CAA97142.1; -; Genomic_DNA.
DR   EMBL; AY558326; AAS56652.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08222.1; -; Genomic_DNA.
DR   PIR; S64438; S64438.
DR   RefSeq; NP_011645.3; NM_001181258.3.
DR   PDB; 5GM6; EM; 3.50 A; f=1-215.
DR   PDB; 5GMK; EM; 3.40 A; I=1-215.
DR   PDB; 5MPS; EM; 3.85 A; y=1-215.
DR   PDB; 5MQ0; EM; 4.17 A; y=1-215.
DR   PDB; 5WSG; EM; 4.00 A; I=1-215.
DR   PDB; 5Y88; EM; 3.70 A; K=1-215.
DR   PDB; 5YLZ; EM; 3.60 A; K=1-215.
DR   PDB; 6BK8; EM; 3.30 A; R=1-215.
DR   PDB; 6EXN; EM; 3.70 A; y=1-215.
DR   PDB; 6J6G; EM; 3.20 A; I=1-215.
DR   PDB; 6J6H; EM; 3.60 A; I=1-215.
DR   PDB; 6J6N; EM; 3.86 A; I=1-215.
DR   PDB; 6J6Q; EM; 3.70 A; I=1-215.
DR   PDBsum; 5GM6; -.
DR   PDBsum; 5GMK; -.
DR   PDBsum; 5MPS; -.
DR   PDBsum; 5MQ0; -.
DR   PDBsum; 5WSG; -.
DR   PDBsum; 5Y88; -.
DR   PDBsum; 5YLZ; -.
DR   PDBsum; 6BK8; -.
DR   PDBsum; 6EXN; -.
DR   PDBsum; 6J6G; -.
DR   PDBsum; 6J6H; -.
DR   PDBsum; 6J6N; -.
DR   PDBsum; 6J6Q; -.
DR   AlphaFoldDB; P53277; -.
DR   EMDB; EMD-0686; -.
DR   EMDB; EMD-0687; -.
DR   EMDB; EMD-0691; -.
DR   EMDB; EMD-0692; -.
DR   EMDB; EMD-3539; -.
DR   EMDB; EMD-3541; -.
DR   EMDB; EMD-3979; -.
DR   EMDB; EMD-6817; -.
DR   EMDB; EMD-6839; -.
DR   EMDB; EMD-7109; -.
DR   EMDB; EMD-9524; -.
DR   EMDB; EMD-9525; -.
DR   SMR; P53277; -.
DR   BioGRID; 33377; 135.
DR   ComplexPortal; CPX-1651; PRP19-associated complex.
DR   ComplexPortal; CPX-1885; NineTeen complex.
DR   DIP; DIP-1684N; -.
DR   IntAct; P53277; 16.
DR   MINT; P53277; -.
DR   STRING; 4932.YGR129W; -.
DR   iPTMnet; P53277; -.
DR   MaxQB; P53277; -.
DR   PaxDb; 4932-YGR129W; -.
DR   PeptideAtlas; P53277; -.
DR   EnsemblFungi; YGR129W_mRNA; YGR129W; YGR129W.
DR   GeneID; 853030; -.
DR   KEGG; sce:YGR129W; -.
DR   AGR; SGD:S000003361; -.
DR   SGD; S000003361; SYF2.
DR   VEuPathDB; FungiDB:YGR129W; -.
DR   eggNOG; KOG2609; Eukaryota.
DR   HOGENOM; CLU_114239_0_0_1; -.
DR   InParanoid; P53277; -.
DR   OMA; YSIREYE; -.
DR   OrthoDB; 2013410at2759; -.
DR   BioCyc; YEAST:G3O-30835-MONOMER; -.
DR   BioGRID-ORCS; 853030; 5 hits in 10 CRISPR screens.
DR   PRO; PR:P53277; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53277; Protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; 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:0071008; C:U2-type post-mRNA release spliceosomal complex; IDA:SGD.
DR   GO; GO:0071004; C:U2-type prespliceosome; IDA:SGD.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR   InterPro; IPR013260; mRNA_splic_SYF2.
DR   Pfam; PF08231; SYF2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Spliceosome.
FT   CHAIN           1..215
FT                   /note="Pre-mRNA-splicing factor SYF2"
FT                   /id="PRO_0000072381"
FT   REGION          36..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          111..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         124
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         125
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   HELIX           97..122
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   STRAND          143..145
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   TURN            147..149
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   STRAND          152..154
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   HELIX           158..187
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   HELIX           198..210
FT                   /evidence="ECO:0007829|PDB:6J6G"
SQ   SEQUENCE   215 AA;  24803 MW;  C80B872FCD808E1D CRC64;
     MDFYKLDEKL KELKRKRVDV SIKSRKLADR EIQEVSANRK PRVYSMEDVN DADESVGDTE
     SPEKEKAFHY TVQEYDAWER RHPQGKTGQS QRGGISYDQL AKLSYEKTLR NLATQTQNSS
     KQDSSADEED NKNVPKKGRI GKVQKDTKTG KITIADDDKL VNKLAVSLQS ESKKRYEARK
     RQMQNAKTLY GVESFINDKN KQFNEKLSRE SKGSE
//