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P32432 (SFP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. 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:
Transcription factor SFP1
Alternative name(s):
Split finger protein 1
Gene names
Name:SFP1
Ordered Locus Names:YLR403W
ORF Names:L8084.4
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length683 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription factor that regulates ribosomal protein (RP) and ribosome biogenesis (Ribi) gene expression in response to nutrients and stress. Promotes RP gene expression under optimal growth conditions. Leaves the nucleus upon environmental challenges, resulting in a down-regulation of RP gene transcription. The effect of the environmental cues on SFP1 localization is mediated through the TOR pathway. Also regulates the expression of genes involved in the G2/M transition during the mitotic cell cycle and the DNA-damage response. Required for carbon-source modulation of cell size. Ref.4 Ref.8 Ref.9 Ref.10 Ref.13

Subunit structure

Interacts with the target of rapamycin complex 1 (TORC1) in a rapamycin-dependent manner. Interacts with MRS6. Ref.13

Subcellular location

Cytoplasm. Nucleus. Note: Nuclear under optimal growth conditions. Leaves the nucleus in response to stress or changes in nutrient availability. The [ISP+] aggregates appear to be nuclear. Ref.4 Ref.6 Ref.9

Domain

The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is unstructured in its native, soluble form, and which forms a parallel in-register beta-sheet in its amyloid form By similarity.

Post-translational modification

Phosphorylated by TORC1 kinase at multiple sites. Phosphorylation regulates nuclear localization and RP promoter binding. Ref.13

Miscellaneous

[ISP+] is the prion form of SFP1. [ISP+] is the result of a conformational change of the cellular SFP1 protein that becomes self-propagating and infectious. This conformational change generates a form of SFP1 that assembles into amyloid fibrils. [ISP+] aggregates accumulate in the nucleus, and results in significantly larger cell size and increased drug resistance (Ref.15). [ISP+] can be cured by GdnHCl (Ref.5). It is speculated that prion properties of transcription factors may generate an optimized phenotypic heterogeneity that buffers yeast populations against diverse environmental insults (Ref.15).

Present with 259 molecules/cell in log phase SD medium.

Sequence similarities

Contains 2 C2H2-type zinc fingers.

Caution

It is uncertain whether Met-1 or Met-6 is the initiator.

Sequence caution

The sequence AAA35041.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MRS6P328644EBI-17035,EBI-14799

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 683683Transcription factor SFP1
PRO_0000046851

Regions

Zinc finger598 – 62326C2H2-type 1
Zinc finger659 – 68325C2H2-type 2
Region230 – 458229Prion domain (PrD)
Compositional bias532 – 55524Poly-Asp

Sequences

Sequence LengthMass (Da)Tools
P32432 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 0332A381D75A6F14

FASTA68374,785
        10         20         30         40         50         60 
MDFTTMTMAS NMATSTTTTA TSAHASINSS SNFNIDIDSN QNTPSILINN NSDSSNGKNT 

        70         80         90        100        110        120 
DFNGVNNIHQ KNIMNNTNNV HLYSPNIMDQ TLLTPQDIAK LRRESIAHSQ GMGGVSWGSI 

       130        140        150        160        170        180 
SVGSWLRDEI ISRRNSIVPA SANGAASAAA SATTTATNTL QIQQPTKRPS VSNPPYHRGY 

       190        200        210        220        230        240 
SISPQIAYTA YLPNLEKQYC KDYSCCGLSL PGLHDLLRHY EEAHISTSPN TTNMSQIPMN 

       250        260        270        280        290        300 
SAGNTSSSVR MTNNTSSANY NLQNNMAANT KNAGHKTNTM QAHSSNATNN TSINNMHANL 

       310        320        330        340        350        360 
QSNMDSNSTI RQSQHPHHQQ NIIQQQLQSN SVNHTSGAVP TPSVMGSATA SSTTANPNVI 

       370        380        390        400        410        420 
SITGAPNSGL SMANHSQQLH LNGNLVDAVS TNDVFLRTSN SPSRHVPHNK QINSNNNSGI 

       430        440        450        460        470        480 
NINNNTSHNS NINMGSKNAM VNRPHTFNNY SLNKTSRNPI QHQSRKIDPH QTDLSPLVLV 

       490        500        510        520        530        540 
QDIDLSFMDD DILGPSNHNS MNSVVNPTTG SHNYNTFHSS VHAKSSQNMV EDQDIDDIDD 

       550        560        570        580        590        600 
DDDVDDDDDD DDDDDTENGS SSNGKSVHNN NYKMPQQAYI DDPARRLYVM DHEEQKPFKC 

       610        620        630        640        650        660 
PVIGCEKTYK NQNGLKYHRL HGHQNQKLHE NPDGTFSVID PDSTDSFGDG MGSAKDKPYR 

       670        680 
CEVCGKRYKN LNGLKYHRGH STH 

« Hide

References

« Hide 'large scale' references
[1]"A split zinc-finger protein is required for normal yeast growth."
Blumberg H., Silver P.
Gene 107:101-110(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [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 SFP1 gene product of Saccharomyces cerevisiae regulates G2/M transitions during the mitotic cell cycle and DNA-damage response."
Xu Z., Norris D.
Genetics 150:1419-1428(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[5]"Novel non-Mendelian determinant involved in the control of translation accuracy in Saccharomyces cerevisiae."
Volkov K.V., Aksenova A.Y., Soom M.J., Osipov K.V., Svitin A.V., Kurischko C., Shkundina I.S., Ter-Avanesyan M.D., Inge-Vechtomov S.G., Mironova L.N.
Genetics 160:25-36(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF PRION FORM.
[6]"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].
[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]"A dynamic transcriptional network communicates growth potential to ribosome synthesis and critical cell size."
Jorgensen P., Rupes I., Sharom J.R., Schneper L., Broach J.R., Tyers M.
Genes Dev. 18:2491-2505(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Sfp1 is a stress- and nutrient-sensitive regulator of ribosomal protein gene expression."
Marion R.M., Regev A., Segal E., Barash Y., Koller D., Friedman N., O'Shea E.K.
Proc. Natl. Acad. Sci. U.S.A. 101:14315-14322(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]"SFP1 is involved in cell size modulation in respiro-fermentative growth conditions."
Cipollina C., Alberghina L., Porro D., Vai M.
Yeast 22:385-399(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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: 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Sfp1 interaction with TORC1 and Mrs6 reveals feedback regulation on TOR signaling."
Lempiainen H., Uotila A., Urban J., Dohnal I., Ammerer G., Loewith R., Shore D.
Mol. Cell 33:704-716(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TORC1 AND MRS6, PHOSPHORYLATION BY TORC1.
[14]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Non-Mendelian determinant [ISP+] in yeast is a nuclear-residing prion form of the global transcriptional regulator Sfp1."
Rogoza T., Goginashvili A., Rodionova S., Ivanov M., Viktorovskaya O., Rubel A., Volkov K., Mironova L.
Proc. Natl. Acad. Sci. U.S.A. 107:10573-10577(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PRION FORMATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63577 Genomic DNA. Translation: AAA35041.1. Different initiation.
U19729 Genomic DNA. Translation: AAB82343.1.
BK006945 Genomic DNA. Translation: DAA09702.1.
PIRJH0497.
RefSeqNP_013507.1. NM_001182291.1.

3D structure databases

ProteinModelPortalP32432.
SMRP32432. Positions 592-681.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31660. 47 interactions.
DIPDIP-1379N.
IntActP32432. 11 interactions.
MINTMINT-410747.
STRING4932.YLR403W.

Proteomic databases

PaxDbP32432.
PeptideAtlasP32432.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR403W; YLR403W; YLR403W.
GeneID851119.
KEGGsce:YLR403W.

Organism-specific databases

CYGDYLR403w.
SGDS000004395. SFP1.

Phylogenomic databases

eggNOGCOG5189.
GeneTreeENSGT00390000003635.
OMANQKLHEN.
OrthoDBEOG7P5TBB.

Enzyme and pathway databases

BioCycYEAST:G3O-32465-MONOMER.

Gene expression databases

GenevestigatorP32432.

Family and domain databases

Gene3D3.30.160.60. 1 hit.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 3 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 2 hits.
PS50157. ZINC_FINGER_C2H2_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio967839.
PROP32432.

Entry information

Entry nameSFP1_YEAST
AccessionPrimary (citable) accession number: P32432
Secondary accession number(s): D6VZ36
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 123 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 XII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families