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P53277 (SYF2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pre-mRNA-splicing factor SYF2
Alternative name(s):
PRP19 complex protein 31
Synthetic lethal with CDC40 protein 2
Gene names
Name:SYF2
Synonyms:NTC31
Ordered Locus Names:YGR129W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.4 Ref.5 Ref.8

Subunit structure

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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Subcellular location

Nucleus Ref.9.

Miscellaneous

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

Sequence similarities

Belongs to the SYF2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 215215Pre-mRNA-splicing factor SYF2
PRO_0000072381

Amino acid modifications

Modified residue451Phosphoserine Ref.12
Modified residue1241Phosphoserine Ref.11 Ref.12 Ref.13
Modified residue1251Phosphoserine Ref.11 Ref.12 Ref.13

Sequences

Sequence LengthMass (Da)Tools
P53277 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: C80B872FCD808E1D

FASTA21524,803
        10         20         30         40         50         60 
MDFYKLDEKL KELKRKRVDV SIKSRKLADR EIQEVSANRK PRVYSMEDVN DADESVGDTE 

        70         80         90        100        110        120 
SPEKEKAFHY TVQEYDAWER RHPQGKTGQS QRGGISYDQL AKLSYEKTLR NLATQTQNSS 

       130        140        150        160        170        180 
KQDSSADEED NKNVPKKGRI GKVQKDTKTG KITIADDDKL VNKLAVSLQS ESKKRYEARK 

       190        200        210 
RQMQNAKTLY GVESFINDKN KQFNEKLSRE SKGSE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
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.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[10]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z72914 Genomic DNA. Translation: CAA97142.1.
AY558326 Genomic DNA. Translation: AAS56652.1.
BK006941 Genomic DNA. Translation: DAA08222.1.
PIRS64438.
RefSeqNP_011645.3. NM_001181258.3.

3D structure databases

ProteinModelPortalP53277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33377. 53 interactions.
DIPDIP-1684N.
IntActP53277. 13 interactions.
MINTMINT-402831.
STRING4932.YGR129W.

Proteomic databases

MaxQBP53277.
PaxDbP53277.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR129W; YGR129W; YGR129W.
GeneID853030.
KEGGsce:YGR129W.

Organism-specific databases

CYGDYGR129w.
SGDS000003361. SYF2.

Phylogenomic databases

eggNOGNOG265019.
HOGENOMHOG000000933.
KOK12868.
OMAHAISIHR.
OrthoDBEOG7SV16F.

Enzyme and pathway databases

BioCycYEAST:G3O-30835-MONOMER.

Gene expression databases

GenevestigatorP53277.

Family and domain databases

InterProIPR013260. mRNA_splic_SYF2.
[Graphical view]
PfamPF08231. SYF2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio972917.

Entry information

Entry nameSYF2_YEAST
AccessionPrimary (citable) accession number: P53277
Secondary accession number(s): D6VUR1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families