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P45976 (FIP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 polyadenylation factor FIP1
Gene names
Name:FIP1
Ordered Locus Names:YJR093C
ORF Names:J1911
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Polymerase-regulating component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Pre-mRNA polyadenylation factor that directly interacts with poly(A) polymerase PAP1. This inhibits the extension of an oligo(A) primer by limiting access of the RNA substrate to the C-terminal RNA binding domain of PAP1. Seems to tether PAP1 to the cleavage factor I. Ref.5

Subunit structure

Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of PTI1, SYC1, SSU72, GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1. In the CPF complex probably interacts directly with PAP1 and YTH1. Interacts with RNA14. Ref.1 Ref.4 Ref.5 Ref.6 Ref.8 Ref.11

Subcellular location

Nucleus Ref.6.

Domain

Circular dichroism measurements suggest that the protein is largely unstructured in the absence of interaction with PAP1. Ref.11

Miscellaneous

Present with 1310 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the FIP1 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PAP1P2946811EBI-6940,EBI-12917
YTH1Q061027EBI-6940,EBI-38049

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 327327Pre-mRNA polyadenylation factor FIP1
PRO_0000215042

Regions

Compositional bias61 – 8020Asp-rich (acidic)
Compositional bias258 – 2669Poly-Asn
Compositional bias284 – 31835Pro-rich

Amino acid modifications

Modified residue501Phosphoserine Ref.9 Ref.10

Secondary structure

......... 327
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P45976 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 471CA2B0CDF99D0A

FASTA32735,777
        10         20         30         40         50         60 
MSSSEDEDDK FLYGSDSELA LPSSKRSRDD EADAGASSNP DIVKRQKFDS PVEETPATAR 

        70         80         90        100        110        120 
DDRSDEDIYS DSSDDDSDSD LEVIISLGPD PTRLDAKLLD SYSTAATSSS KDVISVATDV 

       130        140        150        160        170        180 
SNTITKTSDE RLITEGEANQ GVTATTVKAT ESDGNVPKAM TGSIDLDKEG IFDSVGITTI 

       190        200        210        220        230        240 
DPEVLKEKPW RQPGANLSDY FNYGFNEFTW MEYLHRQEKL QQDYNPRRIL MGLLSLQQQG 

       250        260        270        280        290        300 
KLNSANDTDS NLGNIIDNNN NVNNANMSNL NSNMGNSMSG TPNPPAPPMH PSFPPLPMFG 

       310        320 
SFPPFPMPGM MPPMNQQPNQ NQNQNSK 

« Hide

References

« Hide 'large scale' references
[1]"The FIP1 gene encodes a component of a yeast pre-mRNA polyadenylation factor that directly interacts with poly(A) polymerase."
Preker P.J., Lingner J., Minvielle-Sebastia L., Keller W.
Cell 81:379-389(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INTERACTION WITH PAP1.
[2]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"The WD-repeat protein pfs2p bridges two essential factors within the yeast pre-mRNA 3'-end-processing complex."
Ohnacker M., Barabino S.M.L., Preker P.J., Keller W.
EMBO J. 19:37-47(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PFS2; RNA14 AND YSH1.
[5]"Fip1 regulates the activity of Poly(A) polymerase through multiple interactions."
Helmling S., Zhelkovsky A., Moore C.L.
Mol. Cell. Biol. 21:2026-2037(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PAP1 AND YTH1.
[6]"Organization and function of APT, a subcomplex of the yeast cleavage and polyadenylation factor involved in the formation of mRNA and small nucleolar RNA 3'-ends."
Nedea E., He X., Kim M., Pootoolal J., Zhong G., Canadien V., Hughes T., Buratowski S., Moore C.L., Greenblatt J.
J. Biol. Chem. 278:33000-33010(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CPF COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[7]"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].
[8]"Functional dissection of the zinc finger and flanking domains of the Yth1 cleavage/polyadenylation factor."
Tacahashi Y., Helmling S., Moore C.L.
Nucleic Acids Res. 31:1744-1752(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH YTH1.
[9]"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-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein."
Meinke G., Ezeokonkwo C., Balbo P., Stafford W., Moore C., Bohm A.
Biochemistry 47:6859-6869(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 80-105 IN COMPLEX WITH PAP1, SUBUNIT, DOMAIN, CIRCULAR DICHROISM.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83796 Genomic DNA. Translation: CAA58727.1.
Z49593 Genomic DNA. Translation: CAA89621.1.
BK006943 Genomic DNA. Translation: DAA08877.1.
PIRA56545.
RefSeqNP_012626.1. NM_001181750.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3C66X-ray2.60C/D80-105[»]
DisProtDP00625.
ProteinModelPortalP45976.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33847. 42 interactions.
DIPDIP-2029N.
IntActP45976. 36 interactions.
MINTMINT-383835.
STRING4932.YJR093C.

Proteomic databases

PaxDbP45976.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJR093C; YJR093C; YJR093C.
GeneID853555.
KEGGsce:YJR093C.

Organism-specific databases

CYGDYJR093c.
SGDS000003853. FIP1.

Phylogenomic databases

eggNOGCOG5213.
GeneTreeENSGT00730000111028.
HOGENOMHOG000000819.
KOK14405.
OMATWMEYLH.
OrthoDBEOG7SFJ6V.

Enzyme and pathway databases

BioCycYEAST:G3O-31720-MONOMER.

Gene expression databases

GenevestigatorP45976.

Family and domain databases

InterProIPR007854. Fip1.
[Graphical view]
PfamPF05182. Fip1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP45976.
NextBio974296.
PROP45976.

Entry information

Entry nameFIP1_YEAST
AccessionPrimary (citable) accession number: P45976
Secondary accession number(s): D6VWR1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: March 19, 2014
This is version 103 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 X

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references