SWI4_YEAST
ID SWI4_YEAST Reviewed; 1093 AA.
AC P25302; D3DM17;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Regulatory protein SWI4;
DE AltName: Full=Cell-cycle box factor subunit SWI4;
DE AltName: Full=Protein ART1;
GN Name=SWI4; Synonyms=ART1; OrderedLocusNames=YER111C;
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=2689885; DOI=10.1038/342830a0;
RA Andrews B.J., Herskowitz I.;
RT "The yeast SW14 protein contains a present in developmental regulators and
RT is part of a complex involved in cell-cycle-dependent transcription.";
RL Nature 342:830-833(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 845-1093.
RX PubMed=8355657; DOI=10.1007/bf00277063;
RA Daniel J.;
RT "Potentially rapid walking in cellular regulatory networks using the gene-
RT gene interference method in yeast.";
RL Mol. Gen. Genet. 240:245-257(1993).
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 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 [7]
RP INTERACTION WITH MSA2.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-806, 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: 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 SCB-binding factor
CC (SBF) composed of SWI6 and SWI4. Interacts with MSA2.
CC {ECO:0000269|PubMed:18160399}.
CC -!- INTERACTION:
CC P25302; P25302: SWI4; NbExp=4; IntAct=EBI-18626, EBI-18626;
CC P25302; P09959: SWI6; NbExp=8; IntAct=EBI-18626, EBI-18641;
CC -!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X51606; CAA35949.1; -; Genomic_DNA.
DR EMBL; U18916; AAC03209.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07771.1; -; Genomic_DNA.
DR PIR; S50614; S50614.
DR RefSeq; NP_011036.1; NM_001179001.1.
DR AlphaFoldDB; P25302; -.
DR SMR; P25302; -.
DR BioGRID; 36856; 656.
DR ComplexPortal; CPX-946; SBF transcription complex.
DR DIP; DIP-847N; -.
DR IntAct; P25302; 77.
DR MINT; P25302; -.
DR STRING; 4932.YER111C; -.
DR iPTMnet; P25302; -.
DR MaxQB; P25302; -.
DR PaxDb; P25302; -.
DR PRIDE; P25302; -.
DR EnsemblFungi; YER111C_mRNA; YER111C; YER111C.
DR GeneID; 856847; -.
DR KEGG; sce:YER111C; -.
DR SGD; S000000913; SWI4.
DR VEuPathDB; FungiDB:YER111C; -.
DR eggNOG; ENOG502QUTG; Eukaryota.
DR HOGENOM; CLU_009666_0_0_1; -.
DR InParanoid; P25302; -.
DR OMA; ELCLINT; -.
DR BioCyc; YEAST:G3O-30275-MON; -.
DR ChiTaRS; LDB19; yeast.
DR PRO; PR:P25302; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P25302; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0030907; C:MBF transcription complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0033309; C:SBF transcription complex; IDA:SGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:ComplexPortal.
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 Gene3D; 3.10.260.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR036887; HTH_APSES_sf.
DR InterPro; IPR018004; KilA_N/APSES_HTH.
DR InterPro; IPR029792; Swi4.
DR InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR PANTHER; PTHR43828:SF7; PTHR43828:SF7; 1.
DR Pfam; PF04383; KilA-N; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM01252; KilA-N; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF54616; SSF54616; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS51299; HTH_APSES; 1.
PE 1: Evidence at protein level;
KW ANK repeat; DNA-binding; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..1093
FT /note="Regulatory protein SWI4"
FT /id="PRO_0000067069"
FT DOMAIN 37..147
FT /note="HTH APSES-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT REPEAT 520..549
FT /note="ANK 1"
FT REPEAT 641..670
FT /note="ANK 2"
FT DNA_BIND 71..92
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT REGION 138..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 806
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 175
FT /note="R -> T (in Ref. 1; CAA35949)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="V -> I (in Ref. 1; CAA35949)"
FT /evidence="ECO:0000305"
FT CONFLICT 1054
FT /note="A -> L (in Ref. 1; CAA35949)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1093 AA; 123806 MW; 40EA2EA7732687A9 CRC64;
MPFDVLISNQ KDNTNHQNIT PISKSVLLAP HSNHPVIEIA TYSETDVYEC YIRGFETKIV
MRRTKDDWIN ITQVFKIAQF SKTKRTKILE KESNDMQHEK VQGGYGRFQG TWIPLDSAKF
LVNKYEIIDP VVNSILTFQF DPNNPPPKRS KNSILRKTSP GTKITSPSSY NKTPRKKNSS
SSTSATTTAA NKKGKKNASI NQPNPSPLQN LVFQTPQQFQ VNSSMNIMNN NDNHTTMNFN
NDTRHNLINN ISNNSNQSTI IQQQKSIHEN SFNNNYSATQ KPLQFFPIPT NLQNKNVALN
NPNNNDSNSY SHNIDNVINS SNNNNNGNNN NLIIVPDGPM QSQQQQQHHH EYLTNNFNHS
MMDSITNGNS KKRRKKLNQS NEQQFYNQQE KIQRHFKLMK QPLLWQSFQN PNDHHNEYCD
SNGSNNNNNT VASNGSSIEV FSSNENDNSM NMSSRSMTPF SAGNTSSQNK LENKMTDQEY
KQTILTILSS ERSSDVDQAL LATLYPAPKN FNINFEIDDQ GHTPLHWATA MANIPLIKML
ITLNANALQC NKLGFNCITK SIFYNNCYKE NAFDEIISIL KICLITPDVN GRLPFHYLIE
LSVNKSKNPM IIKSYMDSII LSLGQQDYNL LKICLNYQDN IGNTPLHLSA LNLNFEVYNR
LVYLGASTDI LNLDNESPAS IMNKFNTPAG GSNSRNNNTK ADRKLARNLP QKNYYQQQQQ
QQQPQNNVKI PKIIKTQHPD KEDSTADVNI AKTDSEVNES QYLHSNQPNS TNMNTIMEDL
SNINSFVTSS VIKDIKSTPS KILENSPILY RRRSQSISDE KEKAKDNENQ VEKKKDPLNS
VKTAMPSLES PSSLLPIQMS PLGKYSKPLS QQINKLNTKV SSLQRIMGEE IKNLDNEVVE
TESSISNNKK RLITIAHQIE DAFDSVSNKT PINSISDLQS RIKETSSKLN SEKQNFIQSL
EKSQALKLAT IVQDEESKVD MNTNSSSHPE KQEDEEPIPK STSETSSPKN TKADAKFSNT
VQESYDVNET LRLATELTIL QFKRRMTTLK ISEAKSKINS SVKLDKYRNL IGITIENIDS
KLDDIEKDLR ANA
