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Protein

Flocculation suppression protein

Gene

SFL1

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

Functioni

Involved in cell surface assembly and regulation of the gene related to flocculation (asexual cell aggregation). Mutations in SFL1 causes constitutive cell aggregation.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi64 – 186123By similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • gene silencing Source: SGD
  • negative regulation of flocculation Source: InterPro
  • negative regulation of invasive growth in response to glucose limitation by negative regulation of transcription from RNA polymerase II promoter Source: SGD
  • negative regulation of pseudohyphal growth by negative regulation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33661-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Flocculation suppression protein
Alternative name(s):
Protein SFL1
Gene namesi
Name:SFL1
Ordered Locus Names:YOR140W
ORF Names:YOR3339W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR140W.
SGDiS000005666. SFL1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 766766Flocculation suppression proteinPRO_0000124595Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei220 – 2201PhosphoserineCombined sources
Modified residuei556 – 5561PhosphoserineCombined sources
Modified residuei733 – 7331PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP20134.
PeptideAtlasiP20134.

PTM databases

iPTMnetiP20134.

Interactioni

GO - Molecular functioni

  • RNA polymerase II repressing transcription factor binding Source: SGD

Protein-protein interaction databases

BioGridi34534. 125 interactions.
DIPiDIP-5501N.
IntActiP20134. 2 interactions.
MINTiMINT-537104.

Structurei

3D structure databases

ProteinModelPortaliP20134.
SMRiP20134. Positions 65-136.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

In the N-terminal section; belongs to the HSF family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000075934.
InParanoidiP20134.
OrthoDBiEOG7VMPDV.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR000232. HSF_DNA-bd.
IPR027725. HSF_fam.
IPR027722. Sfl1.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10015. PTHR10015. 3 hits.
PTHR10015:SF197. PTHR10015:SF197. 3 hits.
PfamiPF00447. HSF_DNA-bind. 1 hit.
[Graphical view]
PRINTSiPR00056. HSFDOMAIN.
SMARTiSM00415. HSF. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS00434. HSF_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20134-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEEETVSAP APASTPAPAG TDVGSGGAAA GIANAGAEGG DGAEDVKKHG
60 70 80 90 100
SKMLVGPRPP QNAIFIHKLY QILEDESLHD LIWWTPSGLS FMIKPVERFS
110 120 130 140 150
KALATYFKHT NITSFVRQLN IYGFHKVSHD HSSNDANSGD DANTNDDSNT
160 170 180 190 200
HDDNSGNKNS SGDENTGGGV QEKEKSNPTK IWEFKHSSGI FKKGDIEGLK
210 220 230 240 250
HIKRRASSRN NSSINSRKNS SNQNYDIDSG ARVRPSSIQD PSTSSNSFGN
260 270 280 290 300
FVPQIPGANN SIPEYFNNSH VTYENANHAP LESNNPEMQE QNRPPNFQDE
310 320 330 340 350
TLKHLKEINF DMVKIIESMQ HFISLQHSFC SQSFTFKNVS KKKSENIVKD
360 370 380 390 400
HQKQLQAFES DMLTFKQHVM SRAHRTIDSL CAVNAAATAA SVAPAPAPTS
410 420 430 440 450
TSAYAPKSQY EMMVPPGNQY VPQKSSSTTN IPSRFNTASV PPSQLFVQYQ
460 470 480 490 500
PQSQQHVTYA KQPAHVPNFI NQPIPIQQLP PQYADTFSTP QMMHNPFASK
510 520 530 540 550
NNNKPGNTKR TNSVLMDPLT PAASVGVQGP LNYPIMNINP SVRDYNKPVP
560 570 580 590 600
QNMAPSPIYP INEPTTRLYS QPKMRSLGST SSLPNDRRNS PLKLTPRSSL
610 620 630 640 650
NEDSLYPKPR NSLKSSISGT SLSSSFTLVA NNPAPIRYSQ QGLLRSLNKA
660 670 680 690 700
ANCAPDSVTP LDSSVLTGPP PKNMDNLPAV SSNLINSPMN VEHSSSLSQA
710 720 730 740 750
EPAPQIELPQ PSLPTTSTTK NTGEADNSKR KGSGVYSLLN QEDSSTSSAD
760
PKTEDKAAPA LKKVKM
Length:766
Mass (Da):83,345
Last modified:September 21, 2011 - v3
Checksum:i85D2594DFF42F938
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti446 – 4549FVQYQPQSQ → LYNTNRSRN in CAA64057 (PubMed:9200815).Curated
Sequence conflicti446 – 4549FVQYQPQSQ → LYNTNRSRN in CAA99338 (PubMed:9169874).Curated
Sequence conflicti461 – 4622KQ → SE in CAA64057 (PubMed:9200815).Curated
Sequence conflicti461 – 4622KQ → SE in CAA99338 (PubMed:9169874).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94335 Genomic DNA. Translation: CAA64057.1.
Z75047 Genomic DNA. Translation: CAA99338.1.
BK006948 Genomic DNA. Translation: DAA10912.2.
PIRiS61694.
RefSeqiNP_014783.4. NM_001183559.4.

Genome annotation databases

EnsemblFungiiYOR140W; YOR140W; YOR140W.
GeneIDi854307.
KEGGisce:YOR140W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94335 Genomic DNA. Translation: CAA64057.1.
Z75047 Genomic DNA. Translation: CAA99338.1.
BK006948 Genomic DNA. Translation: DAA10912.2.
PIRiS61694.
RefSeqiNP_014783.4. NM_001183559.4.

3D structure databases

ProteinModelPortaliP20134.
SMRiP20134. Positions 65-136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34534. 125 interactions.
DIPiDIP-5501N.
IntActiP20134. 2 interactions.
MINTiMINT-537104.

PTM databases

iPTMnetiP20134.

Proteomic databases

MaxQBiP20134.
PeptideAtlasiP20134.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR140W; YOR140W; YOR140W.
GeneIDi854307.
KEGGisce:YOR140W.

Organism-specific databases

EuPathDBiFungiDB:YOR140W.
SGDiS000005666. SFL1.

Phylogenomic databases

GeneTreeiENSGT00550000075934.
InParanoidiP20134.
OrthoDBiEOG7VMPDV.

Enzyme and pathway databases

BioCyciYEAST:G3O-33661-MONOMER.

Miscellaneous databases

NextBioi976322.
PROiP20134.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR000232. HSF_DNA-bd.
IPR027725. HSF_fam.
IPR027722. Sfl1.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10015. PTHR10015. 3 hits.
PTHR10015:SF197. PTHR10015:SF197. 3 hits.
PfamiPF00447. HSF_DNA-bind. 1 hit.
[Graphical view]
PRINTSiPR00056. HSFDOMAIN.
SMARTiSM00415. HSF. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS00434. HSF_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Domains of the SFL1 protein of yeasts are homologous to Myc oncoproteins or yeast heat-shock transcription factor."
    Fujita A., Kikuchi Y., Kuhara S., Misumi Y., Matsumoto S., Kobayashi H.
    Gene 85:321-328(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 446-454 AND 461-462.
    Strain: ATCC 204508 / S288c.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  8. "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-556, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-220; SER-556 AND SER-733, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSFL1_YEAST
AccessioniPrimary (citable) accession number: P20134
Secondary accession number(s): D6W2J6, Q99194
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: September 21, 2011
Last modified: May 11, 2016
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1040 molecules/cell in log phase SD medium.1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.