位置:首页 > 蛋白库 > SFL1_YEAST
SFL1_YEAST
ID   SFL1_YEAST              Reviewed;         766 AA.
AC   P20134; D6W2J6; Q99194;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 3.
DT   03-AUG-2022, entry version 190.
DE   RecName: Full=Flocculation suppression protein;
DE   AltName: Full=Protein SFL1;
GN   Name=SFL1; OrderedLocusNames=YOR140W; ORFNames=YOR3339W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2697640; DOI=10.1016/0378-1119(89)90424-1;
RA   Fujita A., Kikuchi Y., Kuhara S., Misumi Y., Matsumoto S., Kobayashi H.;
RT   "Domains of the SFL1 protein of yeasts are homologous to Myc oncoproteins
RT   or yeast heat-shock transcription factor.";
RL   Gene 85:321-328(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9200815;
RX   DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA   Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA   Schwager C., Paces V., Sander C., Ansorge W.;
RT   "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL   Yeast 13:655-672(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [4]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 446-454 AND 461-462.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-556, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-556 AND SER-733, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Involved in cell surface assembly and regulation of the gene
CC       related to flocculation (asexual cell aggregation). Mutations in SFL1
CC       causes constitutive cell aggregation.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 1040 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the HSF family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X94335; CAA64057.1; -; Genomic_DNA.
DR   EMBL; Z75047; CAA99338.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10912.2; -; Genomic_DNA.
DR   PIR; S61694; S61694.
DR   RefSeq; NP_014783.4; NM_001183559.4.
DR   AlphaFoldDB; P20134; -.
DR   SMR; P20134; -.
DR   BioGRID; 34534; 354.
DR   DIP; DIP-5501N; -.
DR   IntAct; P20134; 2.
DR   MINT; P20134; -.
DR   STRING; 4932.YOR140W; -.
DR   iPTMnet; P20134; -.
DR   MaxQB; P20134; -.
DR   PaxDb; P20134; -.
DR   PRIDE; P20134; -.
DR   EnsemblFungi; YOR140W_mRNA; YOR140W; YOR140W.
DR   GeneID; 854307; -.
DR   KEGG; sce:YOR140W; -.
DR   SGD; S000005666; SFL1.
DR   VEuPathDB; FungiDB:YOR140W; -.
DR   eggNOG; KOG0627; Eukaryota.
DR   HOGENOM; CLU_371782_0_0_1; -.
DR   InParanoid; P20134; -.
DR   OMA; DSNTHDD; -.
DR   BioCyc; YEAST:G3O-33661-MON; -.
DR   PRO; PR:P20134; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P20134; protein.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IPI:SGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:SGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0010508; P:positive regulation of autophagy; IDA:SGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR   GO; GO:2001159; P:regulation of protein localization by the Cvt pathway; IDA:SGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR000232; HSF_DNA-bd.
DR   InterPro; IPR027725; HSF_fam.
DR   InterPro; IPR027722; Sfl1.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10015; PTHR10015; 1.
DR   PANTHER; PTHR10015:SF388; PTHR10015:SF388; 1.
DR   Pfam; PF00447; HSF_DNA-bind; 1.
DR   PRINTS; PR00056; HSFDOMAIN.
DR   SMART; SM00415; HSF; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS00434; HSF_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..766
FT                   /note="Flocculation suppression protein"
FT                   /id="PRO_0000124595"
FT   DNA_BIND        64..186
FT                   /evidence="ECO:0000250"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          547..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          657..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..619
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        657..723
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..747
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         220
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         556
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         733
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        446..454
FT                   /note="FVQYQPQSQ -> LYNTNRSRN (in Ref. 2; CAA64057 and 3;
FT                   CAA99338)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        461..462
FT                   /note="KQ -> SE (in Ref. 2; CAA64057 and 3; CAA99338)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   766 AA;  83345 MW;  85D2594DFF42F938 CRC64;
     MSEEETVSAP APASTPAPAG TDVGSGGAAA GIANAGAEGG DGAEDVKKHG SKMLVGPRPP
     QNAIFIHKLY QILEDESLHD LIWWTPSGLS FMIKPVERFS KALATYFKHT NITSFVRQLN
     IYGFHKVSHD HSSNDANSGD DANTNDDSNT HDDNSGNKNS SGDENTGGGV QEKEKSNPTK
     IWEFKHSSGI FKKGDIEGLK HIKRRASSRN NSSINSRKNS SNQNYDIDSG ARVRPSSIQD
     PSTSSNSFGN FVPQIPGANN SIPEYFNNSH VTYENANHAP LESNNPEMQE QNRPPNFQDE
     TLKHLKEINF DMVKIIESMQ HFISLQHSFC SQSFTFKNVS KKKSENIVKD HQKQLQAFES
     DMLTFKQHVM SRAHRTIDSL CAVNAAATAA SVAPAPAPTS TSAYAPKSQY EMMVPPGNQY
     VPQKSSSTTN IPSRFNTASV PPSQLFVQYQ PQSQQHVTYA KQPAHVPNFI NQPIPIQQLP
     PQYADTFSTP QMMHNPFASK NNNKPGNTKR TNSVLMDPLT PAASVGVQGP LNYPIMNINP
     SVRDYNKPVP QNMAPSPIYP INEPTTRLYS QPKMRSLGST SSLPNDRRNS PLKLTPRSSL
     NEDSLYPKPR NSLKSSISGT SLSSSFTLVA NNPAPIRYSQ QGLLRSLNKA ANCAPDSVTP
     LDSSVLTGPP PKNMDNLPAV SSNLINSPMN VEHSSSLSQA EPAPQIELPQ PSLPTTSTTK
     NTGEADNSKR KGSGVYSLLN QEDSSTSSAD PKTEDKAAPA LKKVKM
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024