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P32432

- SFP1_YEAST

UniProt

P32432 - SFP1_YEAST

Protein

Transcription factor SFP1

Gene

SFP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    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.5 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri598 – 62326C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri659 – 68325C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. positive regulation of ribosomal protein gene transcription from RNA polymerase II promoter Source: SGD
    2. positive regulation of transcription from RNA polymerase II promoter Source: SGD
    3. regulation of cell size Source: SGD
    4. response to stress Source: UniProtKB-KW
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Prion

    Keywords - Biological processi

    Stress response, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32465-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor SFP1
    Alternative name(s):
    Split finger protein 1
    Gene namesi
    Name:SFP1
    Ordered Locus Names:YLR403W
    ORF Names:L8084.4
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    CYGDiYLR403w.
    SGDiS000004395. SFP1.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. nucleus Source: SGD

    Keywords - Cellular componenti

    Amyloid, Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 683683Transcription factor SFP1PRO_0000046851Add
    BLAST

    Post-translational modificationi

    Phosphorylated by TORC1 kinase at multiple sites. Phosphorylation regulates nuclear localization and RP promoter binding.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32432.
    PaxDbiP32432.
    PeptideAtlasiP32432.

    Expressioni

    Gene expression databases

    GenevestigatoriP32432.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MRS6P328644EBI-17035,EBI-14799

    Protein-protein interaction databases

    BioGridi31660. 49 interactions.
    DIPiDIP-1379N.
    IntActiP32432. 11 interactions.
    MINTiMINT-410747.
    STRINGi4932.YLR403W.

    Structurei

    3D structure databases

    ProteinModelPortaliP32432.
    SMRiP32432. Positions 592-679.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni230 – 458229Prion domain (PrD)Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi532 – 55524Poly-AspAdd
    BLAST

    Domaini

    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

    Sequence similaritiesi

    Contains 2 C2H2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri598 – 62326C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri659 – 68325C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5189.
    GeneTreeiENSGT00390000003635.
    OMAiNQKLHEN.
    OrthoDBiEOG7P5TBB.

    Family and domain databases

    Gene3Di3.30.160.60. 1 hit.
    InterProiIPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 3 hits.
    [Graphical view]
    PROSITEiPS00028. ZINC_FINGER_C2H2_1. 2 hits.
    PS50157. ZINC_FINGER_C2H2_2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32432-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDFTTMTMAS NMATSTTTTA TSAHASINSS SNFNIDIDSN QNTPSILINN    50
    NSDSSNGKNT DFNGVNNIHQ KNIMNNTNNV HLYSPNIMDQ TLLTPQDIAK 100
    LRRESIAHSQ GMGGVSWGSI SVGSWLRDEI ISRRNSIVPA SANGAASAAA 150
    SATTTATNTL QIQQPTKRPS VSNPPYHRGY SISPQIAYTA YLPNLEKQYC 200
    KDYSCCGLSL PGLHDLLRHY EEAHISTSPN TTNMSQIPMN SAGNTSSSVR 250
    MTNNTSSANY NLQNNMAANT KNAGHKTNTM QAHSSNATNN TSINNMHANL 300
    QSNMDSNSTI RQSQHPHHQQ NIIQQQLQSN SVNHTSGAVP TPSVMGSATA 350
    SSTTANPNVI SITGAPNSGL SMANHSQQLH LNGNLVDAVS TNDVFLRTSN 400
    SPSRHVPHNK QINSNNNSGI NINNNTSHNS NINMGSKNAM VNRPHTFNNY 450
    SLNKTSRNPI QHQSRKIDPH QTDLSPLVLV QDIDLSFMDD DILGPSNHNS 500
    MNSVVNPTTG SHNYNTFHSS VHAKSSQNMV EDQDIDDIDD DDDVDDDDDD 550
    DDDDDTENGS SSNGKSVHNN NYKMPQQAYI DDPARRLYVM DHEEQKPFKC 600
    PVIGCEKTYK NQNGLKYHRL HGHQNQKLHE NPDGTFSVID PDSTDSFGDG 650
    MGSAKDKPYR CEVCGKRYKN LNGLKYHRGH STH 683
    Length:683
    Mass (Da):74,785
    Last modified:October 1, 1993 - v1
    Checksum:i0332A381D75A6F14
    GO

    Sequence cautioni

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63577 Genomic DNA. Translation: AAA35041.1. Different initiation.
    U19729 Genomic DNA. Translation: AAB82343.1.
    BK006945 Genomic DNA. Translation: DAA09702.1.
    PIRiJH0497.
    RefSeqiNP_013507.1. NM_001182291.1.

    Genome annotation databases

    EnsemblFungiiYLR403W; YLR403W; YLR403W.
    GeneIDi851119.
    KEGGisce:YLR403W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63577 Genomic DNA. Translation: AAA35041.1 . Different initiation.
    U19729 Genomic DNA. Translation: AAB82343.1 .
    BK006945 Genomic DNA. Translation: DAA09702.1 .
    PIRi JH0497.
    RefSeqi NP_013507.1. NM_001182291.1.

    3D structure databases

    ProteinModelPortali P32432.
    SMRi P32432. Positions 592-679.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31660. 49 interactions.
    DIPi DIP-1379N.
    IntActi P32432. 11 interactions.
    MINTi MINT-410747.
    STRINGi 4932.YLR403W.

    Proteomic databases

    MaxQBi P32432.
    PaxDbi P32432.
    PeptideAtlasi P32432.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR403W ; YLR403W ; YLR403W .
    GeneIDi 851119.
    KEGGi sce:YLR403W.

    Organism-specific databases

    CYGDi YLR403w.
    SGDi S000004395. SFP1.

    Phylogenomic databases

    eggNOGi COG5189.
    GeneTreei ENSGT00390000003635.
    OMAi NQKLHEN.
    OrthoDBi EOG7P5TBB.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32465-MONOMER.

    Miscellaneous databases

    NextBioi 967839.
    PROi P32432.

    Gene expression databases

    Genevestigatori P32432.

    Family and domain databases

    Gene3Di 3.30.160.60. 1 hit.
    InterProi IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 3 hits.
    [Graphical view ]
    PROSITEi PS00028. ZINC_FINGER_C2H2_1. 2 hits.
    PS50157. ZINC_FINGER_C2H2_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    7. 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.

    Entry informationi

    Entry nameiSFP1_YEAST
    AccessioniPrimary (citable) accession number: P32432
    Secondary accession number(s): D6VZ36
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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 (PubMed:20498075). [ISP+] can be cured by GdnHCl (PubMed:11805042). It is speculated that prion properties of transcription factors may generate an optimized phenotypic heterogeneity that buffers yeast populations against diverse environmental insults (PubMed:20498075).2 Publications
    Present with 259 molecules/cell in log phase SD medium.1 Publication

    Caution

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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3