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SNF6_YEAST
ID   SNF6_YEAST              Reviewed;         332 AA.
AC   P18888; D3DKU3;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 171.
DE   RecName: Full=Transcription regulatory protein SNF6;
DE   AltName: Full=SWI/SNF complex component SNF6;
GN   Name=SNF6; OrderedLocusNames=YHL025W;
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=2188093; DOI=10.1128/mcb.10.6.2544-2553.1990;
RA   Estruch F., Carlson M.;
RT   "SNF6 encodes a nuclear protein that is required for expression of many
RT   genes in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 10:2544-2553(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [3]
RP   GENOME REANNOTATION.
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   [4]
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-165, 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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [7]
RP   3D-STRUCTURE MODELING OF THE SWI/SNF COMPLEX, AND ELECTRON MICROSCOPY OF
RP   THE SWI/SNF COMPLEX.
RX   PubMed=12524530; DOI=10.1038/nsb888;
RA   Smith C.L., Horowitz-Scherer R., Flanagan J.F., Woodcock C.L.,
RA   Peterson C.L.;
RT   "Structural analysis of the yeast SWI/SNF chromatin remodeling complex.";
RL   Nat. Struct. Biol. 10:141-145(2003).
CC   -!- FUNCTION: Involved in transcriptional activation. Component of the
CC       SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which
CC       is required for the positive and negative regulation of gene expression
CC       of a large number of genes. It changes chromatin structure by altering
CC       DNA-histone contacts within a nucleosome, leading eventually to a
CC       change in nucleosome position, thus facilitating or repressing binding
CC       of gene-specific transcription factors.
CC   -!- SUBUNIT: Component of the SWI/SNF global transcription activator
CC       complex. The 1.14 MDa SWI/SNF complex is composed of 11 different
CC       subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73,
CC       ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82;
CC       and three copies of TAF14/SWP29.
CC   -!- INTERACTION:
CC       P18888; P32628: RAD23; NbExp=2; IntAct=EBI-17550, EBI-14668;
CC       P18888; P14736: RAD4; NbExp=2; IntAct=EBI-17550, EBI-14766;
CC       P18888; P38956: SNF11; NbExp=5; IntAct=EBI-17550, EBI-17560;
CC       P18888; P32591: SWI3; NbExp=6; IntAct=EBI-17550, EBI-18622;
CC       P18888; P35189: TAF14; NbExp=4; IntAct=EBI-17550, EBI-18920;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Long;
CC         IsoId=P18888-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=P18888-2; Sequence=Not described;
CC   -!- MISCELLANEOUS: Present with 2900 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: [Isoform Short]: Partially functional. {ECO:0000305}.
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DR   EMBL; M37132; AAA35063.1; -; Genomic_DNA.
DR   EMBL; M32028; AAA35064.1; -; Genomic_DNA.
DR   EMBL; U11582; AAB65078.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06660.1; -; Genomic_DNA.
DR   PIR; A36313; A36313.
DR   RefSeq; NP_011838.1; NM_001179105.1. [P18888-1]
DR   PDB; 6UXV; EM; 4.70 A; I=1-150.
DR   PDB; 6UXW; EM; 8.96 A; I=1-150.
DR   PDB; 7C4J; EM; 2.89 A; C=1-332.
DR   PDB; 7EGM; EM; 3.60 A; I=1-332.
DR   PDB; 7EGP; EM; 6.90 A; I=1-332.
DR   PDBsum; 6UXV; -.
DR   PDBsum; 6UXW; -.
DR   PDBsum; 7C4J; -.
DR   PDBsum; 7EGM; -.
DR   PDBsum; 7EGP; -.
DR   AlphaFoldDB; P18888; -.
DR   SMR; P18888; -.
DR   BioGRID; 36397; 539.
DR   ComplexPortal; CPX-1150; SWI/SNF chromatin remodelling complex.
DR   DIP; DIP-1226N; -.
DR   IntAct; P18888; 39.
DR   MINT; P18888; -.
DR   STRING; 4932.YHL025W; -.
DR   iPTMnet; P18888; -.
DR   MaxQB; P18888; -.
DR   PaxDb; P18888; -.
DR   PRIDE; P18888; -.
DR   EnsemblFungi; YHL025W_mRNA; YHL025W; YHL025W. [P18888-1]
DR   GeneID; 856360; -.
DR   KEGG; sce:YHL025W; -.
DR   SGD; S000001017; SNF6.
DR   VEuPathDB; FungiDB:YHL025W; -.
DR   eggNOG; ENOG502S1YQ; Eukaryota.
DR   HOGENOM; CLU_051557_0_0_1; -.
DR   InParanoid; P18888; -.
DR   OMA; HLLANYI; -.
DR   BioCyc; YEAST:G3O-31045-MON; -.
DR   PRO; PR:P18888; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P18888; protein.
DR   GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0016514; C:SWI/SNF complex; IDA:SGD.
DR   GO; GO:0000182; F:rDNA binding; IDA:SGD.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR   GO; GO:0000470; P:maturation of LSU-rRNA; IMP:SGD.
DR   GO; GO:0006289; P:nucleotide-excision repair; IMP:SGD.
DR   GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IC:ComplexPortal.
DR   GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IMP:SGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative initiation; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..332
FT                   /note="Transcription regulatory protein SNF6"
FT                   /id="PRO_0000072006"
FT   REGION          278..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           2..8
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         165
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   HELIX           70..84
FT                   /evidence="ECO:0007829|PDB:7C4J"
FT   STRAND          90..92
FT                   /evidence="ECO:0007829|PDB:7C4J"
FT   TURN            97..99
FT                   /evidence="ECO:0007829|PDB:7C4J"
FT   HELIX           103..122
FT                   /evidence="ECO:0007829|PDB:7C4J"
FT   STRAND          128..132
FT                   /evidence="ECO:0007829|PDB:7C4J"
FT   HELIX           139..153
FT                   /evidence="ECO:0007829|PDB:7C4J"
FT   HELIX           170..177
FT                   /evidence="ECO:0007829|PDB:7C4J"
FT   STRAND          178..181
FT                   /evidence="ECO:0007829|PDB:7C4J"
FT   HELIX           184..190
FT                   /evidence="ECO:0007829|PDB:7C4J"
FT   STRAND          197..209
FT                   /evidence="ECO:0007829|PDB:7C4J"
FT   HELIX           213..215
FT                   /evidence="ECO:0007829|PDB:7C4J"
FT   HELIX           232..243
FT                   /evidence="ECO:0007829|PDB:7C4J"
SQ   SEQUENCE   332 AA;  37607 MW;  ED9EA9F313F9079F CRC64;
     MGVIKKKRSH HGKASRQQYY SGVQVGGVGS MGAINNNIPS LTSFAEENNY QYGYSGSSAG
     MNGRSLTYAQ QQLNKQRQDF ERVRLRPEQL SNIIHDESDT ISFRSNLLKN FISSNDAFNM
     LSLTTVPCDR IEKSRLFSEK TIRYLMQKQH EMKTQAAELQ EKPLTPLKYT KLIAAAEDGS
     RSTKDMIDAV FEQDSHLRYQ PDGVVVHRDD PALVGKLRGD LREAPADYWT HAYRDVLAQY
     HEAKERIRQK EVTAGEAQDE ASLQQQQQQD LQQQQQVVTT VASQSPHATA TEKEPVPAVV
     DDPLENMFGD YSNEPFNTNF DDEFGDLDAV FF
 
 
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