SWI6_YEAST
ID SWI6_YEAST Reviewed; 803 AA.
AC P09959; D6VYI6;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Regulatory protein SWI6;
DE AltName: Full=Cell-cycle box factor subunit SWI6;
DE AltName: Full=MBF subunit P90;
DE AltName: Full=Trans-acting activator of HO endonuclease gene;
GN Name=SWI6; OrderedLocusNames=YLR182W; ORFNames=L9470.8;
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=2821408; DOI=10.1038/329651a0;
RA Breeden L., Nasmyth K.;
RT "Similarity between cell-cycle genes of budding yeast and fission yeast and
RT the Notch gene of Drosophila.";
RL Nature 329:651-654(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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 CHARACTERIZATION.
RX PubMed=1608451; DOI=10.1038/357508a0;
RA Dirick L., Moll T., Auer H., Nasmyth K.;
RT "A central role for SWI6 in modulating cell cycle Start-specific
RT transcription in yeast.";
RL Nature 357:508-513(1992).
RN [5]
RP INTERACTION WITH STB1.
RX PubMed=10409718; DOI=10.1128/mcb.19.8.5267;
RA Ho Y., Costanzo M., Moore L., Kobayashi R., Andrews B.J.;
RT "Regulation of transcription at the Saccharomyces cerevisiae start
RT transition by Stb1, a Swi6-binding protein.";
RL Mol. Cell. Biol. 19:5267-5278(1999).
RN [6]
RP NUCLEOCYTOPLASMIC SHUTTLING.
RX PubMed=12697814; DOI=10.1128/mcb.23.9.3126-3140.2003;
RA Queralt E., Igual J.C.;
RT "Cell cycle activation of the Swi6p transcription factor is linked to
RT nucleocytoplasmic shuttling.";
RL Mol. Cell. Biol. 23:3126-3140(2003).
RN [7]
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 [8]
RP PHOSPHORYLATION AT SER-160.
RX PubMed=14993267; DOI=10.1128/mcb.24.6.2277-2285.2004;
RA Geymonat M., Spanos A., Wells G.P., Smerdon S.J., Sedgwick S.G.;
RT "Clb6/Cdc28 and Cdc14 regulate phosphorylation status and cellular
RT localization of Swi6.";
RL Mol. Cell. Biol. 24:2277-2285(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-179 AND THR-182, AND
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND SER-547, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [11]
RP INTERACTION WITH MSA1.
RX PubMed=18160399; DOI=10.1074/jbc.m708248200;
RA Ashe M., de Bruin R.A.M., Kalashnikova T., McDonald W.H., Yates J.R. III,
RA Wittenberg C.;
RT "The SBF- and MBF-associated protein Msa1 is required for proper timing of
RT G1-specific transcription in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 283:6040-6049(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-176; THR-179 AND
RP THR-182, AND 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).
RN [14]
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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 188-514.
RX PubMed=10048928; DOI=10.1038/5845;
RA Foord R., Taylor I.A., Sedgwick S.G., Smerdon S.J.;
RT "X-ray structural analysis of the yeast cell cycle regulator Swi6 reveals
RT variations of the ankyrin fold and has implications for Swi6 function.";
RL Nat. Struct. Biol. 6:157-165(1999).
CC -!- FUNCTION: Part of a complex involved in cell-cycle-dependent
CC transcription. SWI4 and SWI6 are required for formation of the cell-
CC cycle box factor-DNA complex. The repeated element in the upstream
CC region of HO (5'-CACGAAAA-3') is called the cell cycle box (CCB).
CC -!- SUBUNIT: Component of the transcription complex MCB-binding factor
CC (MBF) composed of SWI6 and MBP1. Component of the transcription complex
CC SCB-binding factor (SBF) composed of SWI6 and SWI4. Interacts with MSA1
CC and STB1. {ECO:0000269|PubMed:10409718, ECO:0000269|PubMed:18160399}.
CC -!- INTERACTION:
CC P09959; P13365: CLN3; NbExp=2; IntAct=EBI-18641, EBI-4490;
CC P09959; P39678: MBP1; NbExp=4; IntAct=EBI-18641, EBI-10485;
CC P09959; P25302: SWI4; NbExp=8; IntAct=EBI-18641, EBI-18626;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- PTM: Phosphorylated by CDC28 and dephosphorylated by CDC14.
CC {ECO:0000269|PubMed:14993267}.
CC -!- MISCELLANEOUS: Present with 3340 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X06238; CAA29581.1; -; Genomic_DNA.
DR EMBL; U17246; AAB67460.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09502.1; -; Genomic_DNA.
DR PIR; S03161; RGBYW6.
DR RefSeq; NP_013283.1; NM_001182069.1.
DR PDB; 1SW6; X-ray; 2.10 A; A/B=188-512.
DR PDB; 2XFV; X-ray; 1.90 A; A/B=2-126.
DR PDB; 5XW5; X-ray; 1.85 A; C=155-164.
DR PDBsum; 1SW6; -.
DR PDBsum; 2XFV; -.
DR PDBsum; 5XW5; -.
DR AlphaFoldDB; P09959; -.
DR SMR; P09959; -.
DR BioGRID; 31453; 698.
DR ComplexPortal; CPX-946; SBF transcription complex.
DR ComplexPortal; CPX-950; MBP transcription complex.
DR DIP; DIP-598N; -.
DR ELM; P09959; -.
DR IntAct; P09959; 57.
DR MINT; P09959; -.
DR STRING; 4932.YLR182W; -.
DR CarbonylDB; P09959; -.
DR iPTMnet; P09959; -.
DR MaxQB; P09959; -.
DR PaxDb; P09959; -.
DR PRIDE; P09959; -.
DR EnsemblFungi; YLR182W_mRNA; YLR182W; YLR182W.
DR GeneID; 850879; -.
DR KEGG; sce:YLR182W; -.
DR SGD; S000004172; SWI6.
DR VEuPathDB; FungiDB:YLR182W; -.
DR eggNOG; ENOG502QPWC; Eukaryota.
DR GeneTree; ENSGT00940000173997; -.
DR HOGENOM; CLU_017827_0_0_1; -.
DR InParanoid; P09959; -.
DR OMA; DILMGWI; -.
DR BioCyc; YEAST:G3O-32306-MON; -.
DR EvolutionaryTrace; P09959; -.
DR PRO; PR:P09959; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P09959; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0030907; C:MBF transcription complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0033309; C:SBF transcription complex; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:SGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:ComplexPortal.
DR GO; GO:0010845; P:positive regulation of reciprocal meiotic recombination; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; IMP:SGD.
DR GO; GO:0071931; P:positive regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR040822; Swi6_N.
DR Pfam; PF13606; Ank_3; 1.
DR Pfam; PF18530; Swi6_N; 1.
DR SMART; SM00248; ANK; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; ANK repeat; Cytoplasm; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..803
FT /note="Regulatory protein SWI6"
FT /id="PRO_0000067071"
FT REPEAT 318..346
FT /note="ANK 1"
FT REPEAT 347..383
FT /note="ANK 2"
FT REPEAT 384..469
FT /note="ANK 3"
FT REPEAT 470..498
FT /note="ANK 4"
FT REPEAT 499..514
FT /note="ANK 5"
FT REGION 108..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 160
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:14993267,
FT ECO:0007744|PubMed:17287358"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 179
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:2XFV"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:2XFV"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:2XFV"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:2XFV"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:2XFV"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:2XFV"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:2XFV"
FT HELIX 58..68
FT /evidence="ECO:0007829|PDB:2XFV"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2XFV"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:2XFV"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:2XFV"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:2XFV"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2XFV"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1SW6"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:1SW6"
FT HELIX 244..258
FT /evidence="ECO:0007829|PDB:1SW6"
FT HELIX 292..302
FT /evidence="ECO:0007829|PDB:1SW6"
FT HELIX 321..327
FT /evidence="ECO:0007829|PDB:1SW6"
FT HELIX 331..339
FT /evidence="ECO:0007829|PDB:1SW6"
FT HELIX 354..360
FT /evidence="ECO:0007829|PDB:1SW6"
FT HELIX 363..366
FT /evidence="ECO:0007829|PDB:1SW6"
FT HELIX 370..377
FT /evidence="ECO:0007829|PDB:1SW6"
FT HELIX 378..382
FT /evidence="ECO:0007829|PDB:1SW6"
FT HELIX 391..399
FT /evidence="ECO:0007829|PDB:1SW6"
FT HELIX 405..421
FT /evidence="ECO:0007829|PDB:1SW6"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:1SW6"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:1SW6"
FT HELIX 448..452
FT /evidence="ECO:0007829|PDB:1SW6"
FT HELIX 455..461
FT /evidence="ECO:0007829|PDB:1SW6"
FT TURN 462..464
FT /evidence="ECO:0007829|PDB:1SW6"
FT HELIX 473..480
FT /evidence="ECO:0007829|PDB:1SW6"
FT HELIX 483..491
FT /evidence="ECO:0007829|PDB:1SW6"
FT HELIX 506..509
FT /evidence="ECO:0007829|PDB:1SW6"
SQ SEQUENCE 803 AA; 90560 MW; 9B317FCACEEC493C CRC64;
MALEEVVRYL GPHNEIPLTL TRDSETGHFL LKHFLPILQQ YHDTGNINET NPDSFPTDEE
RNKLLAHYGI AVNTDDRGEL WIELEKCLQL LNMLNLFGLF QDAFEFEEPE TDQDEEDPSH
SKLPENKTKS ENSKDNISSK RINNLQDMSL DSDAHRELGS PLKKLKIDTS VIDAESDSTP
NTARGKPNDD INKGPSGDNE NNGTDDNDRT AGPIITFTHD LTSDFLSSPL KIMKALPSPV
VNDNEQKMKL EAFLQRLLFP EIQEMPTSLN NDSSNRNSEG GSSNQQQQHV SFDSLLQEVN
DAFPNTQLNL NIPVDEHGNT PLHWLTSIAN LELVKHLVKH GSNRLYGDNM GESCLVKAVK
SVNNYDSGTF EALLDYLYPC LILEDSMNRT ILHHIIITSG MTGCSAAAKY YLDILMGWIV
KKQNRPIQSG TNEKESKPND KNGERKDSIL ENLDLKWIIA NMLNAQDSNG DTCLNIAARL
GNISIVDALL DYGADPFIAN KSGLRPVDFG AGTSKLQNTN GGDENSKMVS KGDYDGQKNG
KAKKIRSQLL KNPPETTSLI NDVQNLLNSI SKDYENETVQ YNEKLEKLHK ELNEQREELA
NSREQLANVK QLKDEYSLMQ EQLTNLKAGI EEEEESFREE SKKLGIIADE SSGIDWDSSE
YDADEPFKVE FLSDFLEDKL QKNYEGDISK LLEAESKEQI MEQIRNQLPA EKIQSMLPPT
VLLKARINAY KRNDKHLTNV LDTISTKQSE LENKFRRVLS LCLKIDENKV DNMLDGLLQA
ISSEDPQDID TDEMQDFLKK HAS
