SNF5_YEAST
ID SNF5_YEAST Reviewed; 905 AA.
AC P18480; D6VQT4;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=SWI/SNF chromatin-remodeling complex subunit SNF5;
DE AltName: Full=SWI/SNF complex subunit SNF5;
DE AltName: Full=Transcription factor TYE4;
DE AltName: Full=Transcription regulatory protein SNF5;
GN Name=SNF5; Synonyms=SWI10, TYE4; OrderedLocusNames=YBR289W;
GN ORFNames=YBR2036;
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].
RC STRAIN=MCY;
RX PubMed=2233708; DOI=10.1128/mcb.10.11.5616-5625.1990;
RA Laurent B.C., Treitel M.A., Carlson M.;
RT "The SNF5 protein of Saccharomyces cerevisiae is a glutamine- and proline-
RT rich transcriptional activator that affects expression of a broad spectrum
RT of genes.";
RL Mol. Cell. Biol. 10:5616-5625(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091861; DOI=10.1002/yea.320100007;
RA Holmstroem K., Brandt T., Kallesoe T.;
RT "The sequence of a 32,420 bp segment located on the right arm of chromosome
RT II from Saccharomyces cerevisiae.";
RL Yeast 10:S47-S62(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 564.
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-818, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-818, AND IDENTIFICATION BY
RP 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).
RN [9]
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 P18480; P35189: TAF14; NbExp=2; IntAct=EBI-17546, EBI-18920;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 217 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SNF5 family. {ECO:0000305}.
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DR EMBL; M36482; AAA35062.1; -; Genomic_DNA.
DR EMBL; X76053; CAA53652.1; -; Genomic_DNA.
DR EMBL; Z36158; CAA85254.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07404.2; -; Genomic_DNA.
DR PIR; S44551; RGBYS5.
DR RefSeq; NP_009848.4; NM_001178637.4.
DR PDB; 6L9J; X-ray; 2.64 A; A/D/G/J=454-680.
DR PDB; 6UXV; EM; 4.70 A; C=1-905.
DR PDB; 6UXW; EM; 8.96 A; C=1-905.
DR PDB; 7C4J; EM; 2.89 A; F=1-905.
DR PDB; 7EG6; EM; 3.10 A; M=1-905.
DR PDB; 7EGM; EM; 3.60 A; C=1-905.
DR PDB; 7EGP; EM; 6.90 A; C=1-905.
DR PDBsum; 6L9J; -.
DR PDBsum; 6UXV; -.
DR PDBsum; 6UXW; -.
DR PDBsum; 7C4J; -.
DR PDBsum; 7EG6; -.
DR PDBsum; 7EGM; -.
DR PDBsum; 7EGP; -.
DR AlphaFoldDB; P18480; -.
DR SMR; P18480; -.
DR BioGRID; 32983; 510.
DR ComplexPortal; CPX-1150; SWI/SNF chromatin remodelling complex.
DR DIP; DIP-2364N; -.
DR IntAct; P18480; 47.
DR MINT; P18480; -.
DR STRING; 4932.YBR289W; -.
DR iPTMnet; P18480; -.
DR MaxQB; P18480; -.
DR PaxDb; P18480; -.
DR PRIDE; P18480; -.
DR EnsemblFungi; YBR289W_mRNA; YBR289W; YBR289W.
DR GeneID; 852592; -.
DR KEGG; sce:YBR289W; -.
DR SGD; S000000493; SNF5.
DR VEuPathDB; FungiDB:YBR289W; -.
DR eggNOG; KOG1649; Eukaryota.
DR GeneTree; ENSGT00440000038585; -.
DR HOGENOM; CLU_011216_0_0_1; -.
DR InParanoid; P18480; -.
DR OMA; MIQQKHQ; -.
DR BioCyc; YEAST:G3O-29208-MON; -.
DR PRO; PR:P18480; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P18480; protein.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0000228; C:nuclear chromosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:SGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IMP:SGD.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0000436; P:carbon catabolite activation of transcription from RNA polymerase II promoter; IGI:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:SGD.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IC:ComplexPortal.
DR GO; GO:2000219; P:positive regulation of invasive growth in response to glucose limitation; 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.
DR InterPro; IPR006939; SNF5.
DR Pfam; PF04855; SNF5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..905
FT /note="SWI/SNF chromatin-remodeling complex subunit SNF5"
FT /id="PRO_0000205955"
FT REGION 50..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..88
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..109
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 818
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 564
FT /note="D -> E (in Ref. 2; CAA53652 and 3; CAA85254)"
FT /evidence="ECO:0000305"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:7C4J"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 334..356
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 371..399
FT /evidence="ECO:0007829|PDB:7C4J"
FT STRAND 422..428
FT /evidence="ECO:0007829|PDB:7C4J"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 442..449
FT /evidence="ECO:0007829|PDB:7C4J"
FT STRAND 457..464
FT /evidence="ECO:0007829|PDB:6L9J"
FT TURN 466..468
FT /evidence="ECO:0007829|PDB:6L9J"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:6L9J"
FT STRAND 473..480
FT /evidence="ECO:0007829|PDB:6L9J"
FT HELIX 488..495
FT /evidence="ECO:0007829|PDB:6L9J"
FT TURN 496..498
FT /evidence="ECO:0007829|PDB:6L9J"
FT HELIX 506..523
FT /evidence="ECO:0007829|PDB:6L9J"
FT TURN 529..531
FT /evidence="ECO:0007829|PDB:6L9J"
FT STRAND 543..552
FT /evidence="ECO:0007829|PDB:6L9J"
FT STRAND 555..564
FT /evidence="ECO:0007829|PDB:6L9J"
FT HELIX 572..582
FT /evidence="ECO:0007829|PDB:6L9J"
FT HELIX 589..610
FT /evidence="ECO:0007829|PDB:6L9J"
FT STRAND 615..617
FT /evidence="ECO:0007829|PDB:6L9J"
FT HELIX 623..628
FT /evidence="ECO:0007829|PDB:6L9J"
FT STRAND 637..639
FT /evidence="ECO:0007829|PDB:6L9J"
FT HELIX 642..647
FT /evidence="ECO:0007829|PDB:6L9J"
FT STRAND 651..654
FT /evidence="ECO:0007829|PDB:6L9J"
FT HELIX 657..664
FT /evidence="ECO:0007829|PDB:6L9J"
FT HELIX 666..679
FT /evidence="ECO:0007829|PDB:7EG6"
FT STRAND 723..725
FT /evidence="ECO:0007829|PDB:7C4J"
FT STRAND 737..739
FT /evidence="ECO:0007829|PDB:7C4J"
SQ SEQUENCE 905 AA; 102543 MW; F6D31A57E6D6DA94 CRC64;
MNNQPQGTNS VPNSIGNIFS NIGTPSFNMA QIPQQLYQSL TPQQLQMIQQ RHQQLLRSRL
QQQQQQQQQT SPPPQTHQSP PPPPQQSQPI ANQSATSTPP PPPAPHNLHP QIGQVPLAPA
PINLPPQIAQ LPLATQQQVL NKLRQQAIAK NNPQVVNAIT VAQQQVQRQI EQQKGQQTAQ
TQLEQQRQLL VQQQQQQQLR NQIQRQQQQQ FRHHVQIQQQ QQKQQQQQQQ HQQQQQQQQQ
QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQGQ IPQSQQVPQV RSMSGQPPTN VQPTIGQLPQ
LPKLNLPKYQ TIQYDPPETK LPYPTYWSDK KADTDTLLYE QIIQRDKINK YSLIRETNGY
DPFSIYGFSN KEYISRLWHT LKYYQDLKNT RMKSITSTSQ KIPSASIWGN GYSGYGNGIT
NTTTRVIPQV EVGNRKHYLE DKLKVYKQAM NETSEQLVPI RLEFDQDRDR FFLRDTLLWN
KNDKLIKIED FVDDMLRDYR FEDATREQHI DTICQSIQEQ IQEFQGNPYI ELNQDRLGGD
DLRIRIKLDI VVGQNQLIDQ FEWDISNSDN CPEEFAESMC QELELPGEFV TAIAHSIREQ
VHMYHKSLAL LGYNFDGSAI EDDDIRSRML PTITLDDVYR PAAESKIFTP NLLQISAAEL
ERLDKDKDRD TRRKRRQGRS NRRGMLALSG TSASNTSMNG VHNTVAAGNA SSLPPGEILL
PDIADIPRTF RTPVPSTLMP GGVDVGPSVE SYELRNTTTY KSRPDRPKPV SPPCYIIDHI
PGHSLLLSIK LPGKVNTKEE FAAAPNDTSS GTNAMLPSPE SLKTKLNSNI RAGVTIPSIP
NPIANHTVTN SPNPTLQPVI PGGAASKSVP TPSLPIAPPV APHDSEATLL TNSNNGSSNN
NTQNT
