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Pre-mRNA-splicing factor SYF2 (PRP19 complex protein 31) (Synthetic lethal with CDC40 protein 2)

 SYF2_YEAST              Reviewed;         215 AA.
P53277; D6VUR1;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 128.
RecName: Full=Pre-mRNA-splicing factor SYF2;
AltName: Full=PRP19 complex protein 31;
AltName: Full=Synthetic lethal with CDC40 protein 2;
Name=SYF2; Synonyms=NTC31; OrderedLocusNames=YGR129W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[4]
FUNCTION, AND INTERACTION WITH CEF1; CLF1 AND SYF1.
PubMed=11102353;
Ben-Yehuda S., Dix I., Russell C.S., McGarvey M., Beggs J.D.,
Kupiec M.;
"Genetic and physical interactions between factors involved in both
cell cycle progression and pre-mRNA splicing in Saccharomyces
cerevisiae.";
Genetics 156:1503-1517(2000).
[5]
FUNCTION, AND IDENTIFICATION IN THE SPLICEOSOME.
PubMed=11105756; DOI=10.1017/S1355838200000984;
Russell C.S., Ben-Yehuda S., Dix I., Kupiec M., Beggs J.D.;
"Functional analyses of interacting factors involved in both pre-mRNA
splicing and cell cycle progression in Saccharomyces cerevisiae.";
RNA 6:1565-1572(2000).
[6]
IDENTIFICATION IN THE CWC COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=11884590; DOI=10.1128/MCB.22.7.2011-2024.2002;
Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
"Proteomics analysis reveals stable multiprotein complexes in both
fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel
pre-mRNA splicing factors, and snRNAs.";
Mol. Cell. Biol. 22:2011-2024(2002).
[7]
IDENTIFICATION IN THE PRP19-ASSOCIATED COMPLEX.
PubMed=11842115; DOI=10.1093/nar/30.4.1029;
Chen C.-H., Yu W.-C., Tsao T.Y., Wang L.-Y., Chen H.-R., Lin J.-Y.,
Tsai W.-Y., Cheng S.-C.;
"Functional and physical interactions between components of the
Prp19p-associated complex.";
Nucleic Acids Res. 30:1029-1037(2002).
[8]
FUNCTION, AND GENETIC INTERACTION WITH ISY1.
PubMed=12384582; DOI=10.1093/nar/gkf563;
Dahan O., Kupiec M.;
"Mutations in genes of Saccharomyces cerevisiae encoding pre-mRNA
splicing factors cause cell cycle arrest through activation of the
spindle checkpoint.";
Nucleic Acids Res. 30:4361-4370(2002).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-125, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-124 AND SER-125,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-125, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Involved in pre-mRNA splicing and cell cycle control. As
a component of the NTC complex (or PRP19-associated complex),
associates to the spliceosome to mediate conformational
rearrangement or to stabilize the structure of the spliceosome
after U4 snRNA dissociation, which leads to spliceosome
maturation. The cell cycle arrest of SYF2 defective cells may be
due to the inefficient splicing of TUB1.
{ECO:0000269|PubMed:11102353, ECO:0000269|PubMed:11105756,
ECO:0000269|PubMed:12384582}.
-!- SUBUNIT: Belongs to the NTC complex (or PRP19-associated complex),
composed of at least CEF1, CLF1, ISY1, NTC20, SNT309, SYF1, SYF2,
and PRP19. The NTC complex associates with the spliceosome after
the release of the U1 and U4 snRNAs and forms the CWC spliceosome
subcomplex (or CEF1-associated complex) reminiscent of a late-
stage spliceosome composed also of the U2, U5 and U6 snRNAs and at
least BUD13, BUD31, BRR2, CDC40, CUS1, CWC2, CWC15, CWC21, CWC22,
CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, LEA1, MSL1, PRP8,
PRP9, PRP11, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2,
SMD3, SMX2, SMX3, SNU114, SPP2, RSE1 and YJU2. Interacts with
CEF1, CLF1 and SYF1. {ECO:0000269|PubMed:11102353,
ECO:0000269|PubMed:11105756, ECO:0000269|PubMed:11842115,
ECO:0000269|PubMed:11884590}.
-!- INTERACTION:
Q03654:CEF1; NbExp=3; IntAct=EBI-23308, EBI-476;
Q12309:CLF1; NbExp=4; IntAct=EBI-23308, EBI-484;
P38302:NTC20; NbExp=2; IntAct=EBI-23308, EBI-20921;
P32523:PRP19; NbExp=4; IntAct=EBI-23308, EBI-493;
Q04048:SYF1; NbExp=9; IntAct=EBI-23308, EBI-540;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 1670 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the SYF2 family. {ECO:0000305}.
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EMBL; Z72914; CAA97142.1; -; Genomic_DNA.
EMBL; AY558326; AAS56652.1; -; Genomic_DNA.
EMBL; BK006941; DAA08222.1; -; Genomic_DNA.
PIR; S64438; S64438.
RefSeq; NP_011645.3; NM_001181258.3.
PDB; 5GM6; EM; 3.50 A; f=1-215.
PDB; 5GMK; EM; 3.40 A; I=1-215.
PDB; 5MPS; EM; 3.85 A; y=1-215.
PDB; 5MQ0; EM; 4.17 A; y=1-215.
PDB; 5WSG; EM; 4.00 A; I=1-215.
PDBsum; 5GM6; -.
PDBsum; 5GMK; -.
PDBsum; 5MPS; -.
PDBsum; 5MQ0; -.
PDBsum; 5WSG; -.
ProteinModelPortal; P53277; -.
SMR; P53277; -.
BioGrid; 33377; 108.
DIP; DIP-1684N; -.
IntAct; P53277; 20.
MINT; MINT-402831; -.
STRING; 4932.YGR129W; -.
iPTMnet; P53277; -.
MaxQB; P53277; -.
PRIDE; P53277; -.
EnsemblFungi; YGR129W; YGR129W; YGR129W.
GeneID; 853030; -.
KEGG; sce:YGR129W; -.
EuPathDB; FungiDB:YGR129W; -.
SGD; S000003361; SYF2.
HOGENOM; HOG000000933; -.
InParanoid; P53277; -.
KO; K12868; -.
OMA; KPRVYSM; -.
OrthoDB; EOG092C4OA3; -.
BioCyc; YEAST:G3O-30835-MONOMER; -.
PRO; PR:P53277; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0000974; C:Prp19 complex; IDA:SGD.
GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IDA:SGD.
GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:SGD.
GO; GO:0071008; C:U2-type post-mRNA release spliceosomal complex; IDA:SGD.
GO; GO:0071004; C:U2-type prespliceosome; IDA:SGD.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
InterPro; IPR013260; mRNA_splic_SYF2.
Pfam; PF08231; SYF2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; mRNA processing; mRNA splicing;
Nucleus; Phosphoprotein; Reference proteome; Spliceosome.
CHAIN 1 215 Pre-mRNA-splicing factor SYF2.
/FTId=PRO_0000072381.
MOD_RES 45 45 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 124 124 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
HELIX 97 122 {ECO:0000244|PDB:5GMK}.
STRAND 147 149 {ECO:0000244|PDB:5GMK}.
HELIX 161 189 {ECO:0000244|PDB:5GMK}.
HELIX 198 210 {ECO:0000244|PDB:5GMK}.
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


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