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P45976

- FIP1_YEAST

UniProt

P45976 - FIP1_YEAST

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Protein

Pre-mRNA polyadenylation factor FIP1

Gene

FIP1

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

Functioni

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.1 Publication

GO - Molecular functioni

  1. protein binding, bridging Source: SGD

GO - Biological processi

  1. mRNA cleavage Source: SGD
  2. mRNA polyadenylation Source: SGD
Complete GO annotation...

Keywords - Biological processi

mRNA processing

Enzyme and pathway databases

BioCyciYEAST:G3O-31720-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA polyadenylation factor FIP1
Gene namesi
Name:FIP1
Ordered Locus Names:YJR093C
ORF Names:J1911
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome X

Organism-specific databases

CYGDiYJR093c.
SGDiS000003853. FIP1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. mRNA cleavage and polyadenylation specificity factor complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 327327Pre-mRNA polyadenylation factor FIP1PRO_0000215042Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP45976.
PaxDbiP45976.

Expressioni

Gene expression databases

GenevestigatoriP45976.

Interactioni

Subunit structurei

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 RNA14.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PAP1P2946811EBI-6940,EBI-12917
YTH1Q061027EBI-6940,EBI-38049

Protein-protein interaction databases

BioGridi33847. 42 interactions.
DIPiDIP-2029N.
IntActiP45976. 36 interactions.
MINTiMINT-383835.
STRINGi4932.YJR093C.

Structurei

Secondary structure

1
327
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi83 – 853
Beta strandi87 – 904
Beta strandi93 – 953
Helixi96 – 983
Helixi99 – 1024

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3C66X-ray2.60C/D80-105[»]
DisProtiDP00625.
ProteinModelPortaliP45976.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45976.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi61 – 8020Asp-rich (acidic)Add
BLAST
Compositional biasi258 – 2669Poly-Asn
Compositional biasi284 – 31835Pro-richAdd
BLAST

Domaini

Circular dichroism measurements suggest that the protein is largely unstructured in the absence of interaction with PAP1.1 Publication

Sequence similaritiesi

Belongs to the FIP1 family.Curated

Phylogenomic databases

eggNOGiCOG5213.
GeneTreeiENSGT00730000111028.
HOGENOMiHOG000000819.
InParanoidiP45976.
KOiK14405.
OMAiTWMEYLH.
OrthoDBiEOG7SFJ6V.

Family and domain databases

InterProiIPR007854. Fip1.
[Graphical view]
PfamiPF05182. Fip1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P45976 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSSEDEDDK FLYGSDSELA LPSSKRSRDD EADAGASSNP DIVKRQKFDS
60 70 80 90 100
PVEETPATAR DDRSDEDIYS DSSDDDSDSD LEVIISLGPD PTRLDAKLLD
110 120 130 140 150
SYSTAATSSS KDVISVATDV SNTITKTSDE RLITEGEANQ GVTATTVKAT
160 170 180 190 200
ESDGNVPKAM TGSIDLDKEG IFDSVGITTI DPEVLKEKPW RQPGANLSDY
210 220 230 240 250
FNYGFNEFTW MEYLHRQEKL QQDYNPRRIL MGLLSLQQQG KLNSANDTDS
260 270 280 290 300
NLGNIIDNNN NVNNANMSNL NSNMGNSMSG TPNPPAPPMH PSFPPLPMFG
310 320
SFPPFPMPGM MPPMNQQPNQ NQNQNSK
Length:327
Mass (Da):35,777
Last modified:November 1, 1995 - v1
Checksum:i471CA2B0CDF99D0A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83796 Genomic DNA. Translation: CAA58727.1.
Z49593 Genomic DNA. Translation: CAA89621.1.
BK006943 Genomic DNA. Translation: DAA08877.1.
PIRiA56545.
RefSeqiNP_012626.1. NM_001181750.1.

Genome annotation databases

EnsemblFungiiYJR093C; YJR093C; YJR093C.
GeneIDi853555.
KEGGisce:YJR093C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83796 Genomic DNA. Translation: CAA58727.1 .
Z49593 Genomic DNA. Translation: CAA89621.1 .
BK006943 Genomic DNA. Translation: DAA08877.1 .
PIRi A56545.
RefSeqi NP_012626.1. NM_001181750.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3C66 X-ray 2.60 C/D 80-105 [» ]
DisProti DP00625.
ProteinModelPortali P45976.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33847. 42 interactions.
DIPi DIP-2029N.
IntActi P45976. 36 interactions.
MINTi MINT-383835.
STRINGi 4932.YJR093C.

Proteomic databases

MaxQBi P45976.
PaxDbi P45976.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YJR093C ; YJR093C ; YJR093C .
GeneIDi 853555.
KEGGi sce:YJR093C.

Organism-specific databases

CYGDi YJR093c.
SGDi S000003853. FIP1.

Phylogenomic databases

eggNOGi COG5213.
GeneTreei ENSGT00730000111028.
HOGENOMi HOG000000819.
InParanoidi P45976.
KOi K14405.
OMAi TWMEYLH.
OrthoDBi EOG7SFJ6V.

Enzyme and pathway databases

BioCyci YEAST:G3O-31720-MONOMER.

Miscellaneous databases

EvolutionaryTracei P45976.
NextBioi 974296.
PROi P45976.

Gene expression databases

Genevestigatori P45976.

Family and domain databases

InterProi IPR007854. Fip1.
[Graphical view ]
Pfami PF05182. Fip1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiFIP1_YEAST
AccessioniPrimary (citable) accession number: P45976
Secondary accession number(s): D6VWR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 107 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 1310 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3