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Protein

Pre-mRNA-splicing factor SYF2

Gene

SYF2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 TUB1.3 Publications

GO - Biological processi

  • mRNA splicing, via spliceosome Source: SGD
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Enzyme and pathway databases

BioCyciYEAST:G3O-30835-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-splicing factor SYF2
Alternative name(s):
PRP19 complex protein 31
Synthetic lethal with CDC40 protein 2
Gene namesi
Name:SYF2
Synonyms:NTC31
Ordered Locus Names:YGR129W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGR129w.
EuPathDBiFungiDB:YGR129W.
SGDiS000003361. SYF2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • nucleus Source: SGD
  • Prp19 complex Source: SGD
  • U2-type catalytic step 1 spliceosome Source: SGD
  • U2-type catalytic step 2 spliceosome Source: SGD
  • U2-type post-mRNA release spliceosomal complex Source: SGD
  • U2-type prespliceosome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Pre-mRNA-splicing factor SYF2PRO_0000072381Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei45 – 451Phosphoserine1 Publication
Modified residuei124 – 1241Phosphoserine3 Publications
Modified residuei125 – 1251Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53277.
PaxDbiP53277.

Expressioni

Gene expression databases

GenevestigatoriP53277.

Interactioni

Subunit structurei

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 SYF1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CEF1Q036543EBI-23308,EBI-476
CLF1Q123092EBI-23308,EBI-484
NTC20P383022EBI-23308,EBI-20921
PRP19P325234EBI-23308,EBI-493
SYF1Q040484EBI-23308,EBI-540

Protein-protein interaction databases

BioGridi33377. 55 interactions.
DIPiDIP-1684N.
IntActiP53277. 13 interactions.
MINTiMINT-402831.
STRINGi4932.YGR129W.

Structurei

3D structure databases

ProteinModelPortaliP53277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SYF2 family.Curated

Phylogenomic databases

eggNOGiNOG265019.
HOGENOMiHOG000000933.
InParanoidiP53277.
KOiK12868.
OMAiVERDIAM.
OrthoDBiEOG7SV16F.

Family and domain databases

InterProiIPR013260. mRNA_splic_SYF2.
[Graphical view]
PfamiPF08231. SYF2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53277-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDFYKLDEKL KELKRKRVDV SIKSRKLADR EIQEVSANRK PRVYSMEDVN
60 70 80 90 100
DADESVGDTE SPEKEKAFHY TVQEYDAWER RHPQGKTGQS QRGGISYDQL
110 120 130 140 150
AKLSYEKTLR NLATQTQNSS KQDSSADEED NKNVPKKGRI GKVQKDTKTG
160 170 180 190 200
KITIADDDKL VNKLAVSLQS ESKKRYEARK RQMQNAKTLY GVESFINDKN
210
KQFNEKLSRE SKGSE
Length:215
Mass (Da):24,803
Last modified:October 1, 1996 - v1
Checksum:iC80B872FCD808E1D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72914 Genomic DNA. Translation: CAA97142.1.
AY558326 Genomic DNA. Translation: AAS56652.1.
BK006941 Genomic DNA. Translation: DAA08222.1.
PIRiS64438.
RefSeqiNP_011645.3. NM_001181258.3.

Genome annotation databases

EnsemblFungiiYGR129W; YGR129W; YGR129W.
GeneIDi853030.
KEGGisce:YGR129W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72914 Genomic DNA. Translation: CAA97142.1.
AY558326 Genomic DNA. Translation: AAS56652.1.
BK006941 Genomic DNA. Translation: DAA08222.1.
PIRiS64438.
RefSeqiNP_011645.3. NM_001181258.3.

3D structure databases

ProteinModelPortaliP53277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33377. 55 interactions.
DIPiDIP-1684N.
IntActiP53277. 13 interactions.
MINTiMINT-402831.
STRINGi4932.YGR129W.

Proteomic databases

MaxQBiP53277.
PaxDbiP53277.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR129W; YGR129W; YGR129W.
GeneIDi853030.
KEGGisce:YGR129W.

Organism-specific databases

CYGDiYGR129w.
EuPathDBiFungiDB:YGR129W.
SGDiS000003361. SYF2.

Phylogenomic databases

eggNOGiNOG265019.
HOGENOMiHOG000000933.
InParanoidiP53277.
KOiK12868.
OMAiVERDIAM.
OrthoDBiEOG7SV16F.

Enzyme and pathway databases

BioCyciYEAST:G3O-30835-MONOMER.

Miscellaneous databases

NextBioi972917.
PROiP53277.

Gene expression databases

GenevestigatoriP53277.

Family and domain databases

InterProiIPR013260. mRNA_splic_SYF2.
[Graphical view]
PfamiPF08231. SYF2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    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.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Genetic and physical interactions between factors involved in both cell cycle progression and pre-mRNA splicing in Saccharomyces cerevisiae."
    Ben-Yehuda S., Dix I., Russell C.S., McGarvey M., Beggs J.D., Kupiec M.
    Genetics 156:1503-1517(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CEF1; CLF1 AND SYF1.
  5. "Functional analyses of interacting factors involved in both pre-mRNA splicing and cell cycle progression in Saccharomyces cerevisiae."
    Russell C.S., Ben-Yehuda S., Dix I., Kupiec M., Beggs J.D.
    RNA 6:1565-1572(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE SPLICEOSOME.
  6. "Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs."
    Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.
    Mol. Cell. Biol. 22:2011-2024(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CWC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Functional and physical interactions between components of the Prp19p-associated complex."
    Chen C.-H., Yu W.-C., Tsao T.Y., Wang L.-Y., Chen H.-R., Lin J.-Y., Tsai W.-Y., Cheng S.-C.
    Nucleic Acids Res. 30:1029-1037(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE PRP19-ASSOCIATED COMPLEX.
  8. "Mutations in genes of Saccharomyces cerevisiae encoding pre-mRNA splicing factors cause cell cycle arrest through activation of the spindle checkpoint."
    Dahan O., Kupiec M.
    Nucleic Acids Res. 30:4361-4370(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, GENETIC INTERACTION WITH ISY1.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  12. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-124 AND SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYF2_YEAST
AccessioniPrimary (citable) accession number: P53277
Secondary accession number(s): D6VUR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 27, 2015
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1670 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.