Transcription factor SFP1 - SFP1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P32432 (SFP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 125. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Transcription factor SFP1

Alternative name(s):
Split finger protein 1

Gene names

Name:	SFP1
Ordered Locus Names:	YLR403W
ORF Names:	L8084.4

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	683 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Stress response Transcription Transcription regulation
Cellular component	Amyloid Cytoplasm Nucleus
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Prion
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of ribosomal protein gene transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 14555489 Ref.9 Ref.8. Source: SGD positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 12089449 Ref.4. Source: SGD regulation of cell size Inferred from mutant phenotype Ref.8 Ref.10. Source: SGD response to stress Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-templated Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay Ref.9 Ref.8. Source: SGD nucleus Inferred from direct assay Ref.9 Ref.8 Ref.4. Source: SGD
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction PubMed 16429126 PubMed 18467557 PubMed 21179020. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MRS6	P32864	4	EBI-17035,EBI-14799

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 683

683

Transcription factor SFP1

PRO_0000046851

Regions

Zinc finger

598 – 623

C2H2-type 1

Zinc finger

659 – 683

C2H2-type 2

Region

230 – 458

229

Prion domain (PrD)

Compositional bias

532 – 555

Poly-Asp

Sequences

Sequence

Length

Mass (Da)

Tools

P32432 [UniParc].

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

FASTA

683

74,785

        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' referencesShow '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. 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]	"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.
[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.
PIR	JH0497.
RefSeq	NP_013507.1. NM_001182291.1.
3D structure databases
ProteinModelPortal	P32432.
SMR	P32432. Positions 592-679.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	31660. 49 interactions.
DIP	DIP-1379N.
IntAct	P32432. 11 interactions.
MINT	MINT-410747.
STRING	4932.YLR403W.
Proteomic databases
MaxQB	P32432.
PaxDb	P32432.
PeptideAtlas	P32432.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR403W; YLR403W; YLR403W.
GeneID	851119.
KEGG	sce:YLR403W.
Organism-specific databases
CYGD	YLR403w.
SGD	S000004395. SFP1.
Phylogenomic databases
eggNOG	COG5189.
GeneTree	ENSGT00390000003635.
OMA	NQKLHEN.
OrthoDB	EOG7P5TBB.
Enzyme and pathway databases
BioCyc	YEAST:G3O-32465-MONOMER.
Gene expression databases
Genevestigator	P32432.
Family and domain databases
Gene3D	3.30.160.60. 1 hit.
InterPro	IPR007087. Znf_C2H2. IPR015880. Znf_C2H2-like. IPR013087. Znf_C2H2/integrase_DNA-bd. [Graphical view]
SMART	SM00355. ZnF_C2H2. 3 hits. [Graphical view]
PROSITE	PS00028. ZINC_FINGER_C2H2_1. 2 hits. PS50157. ZINC_FINGER_C2H2_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	967839.
PRO	P32432.

Entry information

Entry name

SFP1_YEAST

Accession

Primary (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:	June 11, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal 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

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents