SWI3_YEAST
ID SWI3_YEAST Reviewed; 825 AA.
AC P32591; D6VW13;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=SWI/SNF complex subunit SWI3;
DE AltName: Full=Transcription factor TYE2;
DE AltName: Full=Transcription regulatory protein SWI3;
GN Name=SWI3; Synonyms=TYE2; OrderedLocusNames=YJL176C; ORFNames=J0495;
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=1339306; DOI=10.1016/0092-8674(92)90192-f;
RA Peterson C.L., Herskowitz I.;
RT "Characterization of the yeast SWI1, SWI2, and SWI3 genes, which encode a
RT global activator of transcription.";
RL Cell 68:573-583(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8221926; DOI=10.1007/bf00351791;
RA Loehning C., Rosenbaum C., Ciriacy M.;
RT "Isolation of the TYE2 gene reveals its identity to SWI3 encoding a general
RT transcription factor in Saccharomyces cerevisiae.";
RL Curr. Genet. 24:193-199(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-185 AND SER-657, AND
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-235, 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 [8]
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).
RN [9]
RP INTERACTION WITH RTT102.
RX PubMed=15506919; DOI=10.1042/bst0320899;
RA Lee K.K., Prochasson P., Florens L., Swanson S.K., Washburn M.P.,
RA Workman J.L.;
RT "Proteomic analysis of chromatin-modifying complexes in Saccharomyces
RT cerevisiae identifies novel subunits.";
RL Biochem. Soc. Trans. 32:899-903(2004).
RN [10]
RP INTERACTION WITH SWP82.
RX PubMed=16204215; DOI=10.1534/genetics.105.047589;
RA Wilson B., Erdjument-Bromage H., Tempst P., Cairns B.R.;
RT "The RSC chromatin remodeling complex bears an essential fungal-specific
RT protein module with broad functional roles.";
RL Genetics 172:795-809(2006).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 311-395, AND MUTAGENESIS OF
RP ASP-374; LYS-383; LYS-387 AND ASN-392.
RX PubMed=16461455; DOI=10.1073/pnas.0510949103;
RA Da G., Lenkart J., Zhao K., Shiekhattar R., Cairns B.R., Marmorstein R.;
RT "Structure and function of the SWIRM domain, a conserved protein module
RT found in chromatin regulatory complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:2057-2062(2006).
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: Interacts with RTT102, SWP82 and the N-terminus of SNF2.
CC Component of the SWI/SNF global transcription activator complex. The
CC 1.14 MDa SWI/SNF complex is composed of 11 different subunits: one copy
CC each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two
CC copies each of SWI3, SNF6, SNF11, SWP82; and three copies of
CC TAF14/SWP29. {ECO:0000269|PubMed:15506919,
CC ECO:0000269|PubMed:16204215}.
CC -!- INTERACTION:
CC P32591; P53330: RTT102; NbExp=2; IntAct=EBI-18622, EBI-23637;
CC P32591; P22082: SNF2; NbExp=8; IntAct=EBI-18622, EBI-17526;
CC P32591; P18888: SNF6; NbExp=6; IntAct=EBI-18622, EBI-17550;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 3150 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M84390; AAA35136.1; -; Genomic_DNA.
DR EMBL; X56792; CAA40112.1; -; Genomic_DNA.
DR EMBL; Z49451; CAA89470.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08629.1; -; Genomic_DNA.
DR PIR; S26706; S26706.
DR RefSeq; NP_012359.1; NM_001181609.1.
DR PDB; 2FQ3; X-ray; 1.40 A; A=309-398.
DR PDB; 6L9J; X-ray; 2.64 A; B/C/E/F/H/I/K/L=212-398.
DR PDB; 6UXV; EM; 4.70 A; D/E/F/G=1-825.
DR PDB; 6UXW; EM; 8.96 A; D/E/F/G=1-825.
DR PDB; 7C4J; EM; 2.89 A; B/D=1-825.
DR PDB; 7EGM; EM; 3.60 A; D/E=1-825.
DR PDB; 7EGP; EM; 6.90 A; D/E=1-825.
DR PDBsum; 2FQ3; -.
DR PDBsum; 6L9J; -.
DR PDBsum; 6UXV; -.
DR PDBsum; 6UXW; -.
DR PDBsum; 7C4J; -.
DR PDBsum; 7EGM; -.
DR PDBsum; 7EGP; -.
DR AlphaFoldDB; P32591; -.
DR SMR; P32591; -.
DR BioGRID; 33585; 415.
DR ComplexPortal; CPX-1150; SWI/SNF chromatin remodelling complex.
DR DIP; DIP-2471N; -.
DR IntAct; P32591; 48.
DR MINT; P32591; -.
DR STRING; 4932.YJL176C; -.
DR iPTMnet; P32591; -.
DR MaxQB; P32591; -.
DR PaxDb; P32591; -.
DR PRIDE; P32591; -.
DR EnsemblFungi; YJL176C_mRNA; YJL176C; YJL176C.
DR GeneID; 853264; -.
DR KEGG; sce:YJL176C; -.
DR SGD; S000003712; SWI3.
DR VEuPathDB; FungiDB:YJL176C; -.
DR eggNOG; KOG1279; Eukaryota.
DR GeneTree; ENSGT00940000172343; -.
DR HOGENOM; CLU_004447_2_3_1; -.
DR InParanoid; P32591; -.
DR OMA; FYRYWSA; -.
DR BioCyc; YEAST:G3O-31611-MON; -.
DR Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR EvolutionaryTrace; P32591; -.
DR PRO; PR:P32591; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P32591; 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:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0042393; F:histone binding; IPI:SGD.
DR GO; GO:0000436; P:carbon catabolite activation of transcription from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IC:ComplexPortal.
DR GO; GO:0031496; P:positive regulation of mating type switching; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR CDD; cd00167; SANT; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR032451; SMARCC_C.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF04433; SWIRM; 1.
DR Pfam; PF16495; SWIRM-assoc_1; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..825
FT /note="SWI/SNF complex subunit SWI3"
FT /id="PRO_0000197123"
FT DOMAIN 305..402
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT DOMAIN 522..573
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 1..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..722
FT /note="Leucine-zipper"
FT COMPBIAS 1..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..208
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 374
FT /note="D->A: Loss of DNA-binding."
FT /evidence="ECO:0000269|PubMed:16461455"
FT MUTAGEN 383
FT /note="K->D: Loss of DNA-binding; when associated with D-
FT 387."
FT /evidence="ECO:0000269|PubMed:16461455"
FT MUTAGEN 387
FT /note="K->D: Loss of DNA-binding; when associated with D-
FT 383."
FT /evidence="ECO:0000269|PubMed:16461455"
FT MUTAGEN 392
FT /note="N->A: Loss of DNA-binding."
FT /evidence="ECO:0000269|PubMed:16461455"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:6L9J"
FT HELIX 321..326
FT /evidence="ECO:0007829|PDB:2FQ3"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:2FQ3"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:6L9J"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 340..356
FT /evidence="ECO:0007829|PDB:2FQ3"
FT HELIX 364..370
FT /evidence="ECO:0007829|PDB:2FQ3"
FT HELIX 375..387
FT /evidence="ECO:0007829|PDB:2FQ3"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:2FQ3"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 438..443
FT /evidence="ECO:0007829|PDB:7C4J"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 452..467
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 519..521
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 529..541
FT /evidence="ECO:0007829|PDB:7C4J"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 546..553
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 558..567
FT /evidence="ECO:0007829|PDB:7C4J"
FT TURN 572..574
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 590..594
FT /evidence="ECO:0007829|PDB:7C4J"
FT TURN 602..604
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 606..614
FT /evidence="ECO:0007829|PDB:7C4J"
FT TURN 615..617
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 620..639
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 641..644
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 649..665
FT /evidence="ECO:0007829|PDB:7C4J"
FT TURN 668..670
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 674..740
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 743..746
FT /evidence="ECO:0007829|PDB:7C4J"
FT HELIX 762..775
FT /evidence="ECO:0007829|PDB:7C4J"
FT STRAND 781..784
FT /evidence="ECO:0007829|PDB:7C4J"
SQ SEQUENCE 825 AA; 92926 MW; DBA2E2022F15F9A6 CRC64;
MENTLGEGST VNASVDVDQH GNDNNSDSNA NAAVAGVANT DTAGEESQQQ DESLKDEATV
PNTRDAESEA ITVTAKQQPT MQANKLDSQE TPSTEESRAQ NVFGQDNEDS DNLFGETESS
VSNNEANTPS IPTNPVDNEN NKPAIKEDST IQDSNGDVKN MEDVKIQKEE EPENNTVIEG
VKEESQPDEN TKEMDEVEED DEDDDQPMIS PDNSIFGDTK SESKQLGNTS SVANTPSEIP
DAHKAEQEDI IEKTESVDKK VDSGEERNEQ EREIMNDHSK SANPKKTTIT RVEPETFEIP
QAHEIVIPSY SKWFNLEKIH SIEVQSLPEF FTNRIPSKTP EVYMRYRNFM VNSYRLNPNE
YFSVTTARRN VSGDAAALFR LHKFLTKWGL INYQVDSKLL PKNIEPPLTS QYSTRHDAPR
GLFPFESYKP SVQLPDMAKL KKMMNTSDSE STLYKYLKES KRKYDEITHP PSTTDDENGD
KNDNGGKMNN EVSTSTSMTG DANLLEEGET SRPLKKVKIL EQIDENWSKE DLQKLLKGIQ
EFGADWYKVA KNVGNKSPEQ CILRFLQLPI EDKFLYGDGN GKGDNDNGLG PLKYAPHLPF
SKSENPVLST IAFLVGLVNP KTVQSMTQRA IQSAESIKSQ KEEISDQKPI EHIKEGSEIA
ISSLGYRSHI FATNEERQMN FLTNELIRLQ MEKLDAKLNH LKKLEKFMEL ERKTLERQQE
NLLIQRLNFN QNSSKIVNVL SKCLNLISDS NINNSSVAEK EEIRSQIDHF KSMLSKPETL
SIGKNPFNKP NIETGENHNG QSISNENDVK PISIEAPQFY RYWSA
