SWI5_YEAST
ID SWI5_YEAST Reviewed; 709 AA.
AC P08153; D6VSC9; E9P945;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 228.
DE RecName: Full=Transcriptional factor SWI5;
GN Name=SWI5; OrderedLocusNames=YDR146C; ORFNames=YD8358.03C;
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=3284746; DOI=10.1002/j.1460-2075.1988.tb02836.x;
RA Stillman D.J., Bankier A.T., Seddon A., Groenhout E.G., Nasmyth K.A.;
RT "Characterization of a transcription factor involved in mother cell
RT specific transcription of the yeast HO gene.";
RL EMBO J. 7:485-494(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP DNA-BINDING.
RX PubMed=2831463; DOI=10.1038/332284a0;
RA Nagai K., Nakaseko Y., Nasmyth K.A., Rhodes D.;
RT "Zinc-finger motifs expressed in E. coli and folded in vitro direct
RT specific binding to DNA.";
RL Nature 332:284-286(1988).
RN [6]
RP PHOSPHORYLATION AT SER-522; SER-646 AND SER-664 BY CDC28, MUTAGENESIS, AND
RP SUBCELLULAR LOCATION.
RX PubMed=1652372; DOI=10.1016/0092-8674(91)90118-i;
RA Moll T., Tebb G., Surana U., Robitsch H., Nasmyth K.;
RT "The role of phosphorylation and the CDC28 protein kinase in cell cycle-
RT regulated nuclear import of the S. cerevisiae transcription factor SWI5.";
RL Cell 66:743-758(1991).
RN [7]
RP PHOSPHORYLATION BY PHO85.
RX PubMed=10692159; DOI=10.1046/j.1365-2958.2000.01754.x;
RA Measday V., McBride H., Moffat J., Stillman D., Andrews B.J.;
RT "Interactions between Pho85 cyclin-dependent kinase complexes and the Swi5
RT transcription factor in budding yeast.";
RL Mol. Microbiol. 35:825-834(2000).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505 AND SER-646, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492 AND SER-505, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225; SER-278; SER-300;
RP THR-339; SER-376; SER-488; SER-492 AND SER-522, AND IDENTIFICATION BY MASS
RP 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 [12]
RP STRUCTURE BY NMR OF 540-608.
RX PubMed=1453468; DOI=10.1016/0022-2836(92)90846-c;
RA Neuhaus D., Nakaseko Y., Schwabe J.W.R., Klug A.;
RT "Solution structures of two zinc-finger domains from SWI5 obtained using
RT two-dimensional 1H nuclear magnetic resonance spectroscopy. A zinc-finger
RT structure with a third strand of beta-sheet.";
RL J. Mol. Biol. 228:637-651(1992).
CC -!- FUNCTION: Determines the mother-cell-specific transcription of the HO
CC endonuclease gene that is responsible for the initiation of mating-type
CC switching in yeast. Recognizes a specific sequence in the promoter of
CC the HO gene. Activates EGT2 transcription in a concentration-dependent
CC manner. Synthesized during G2 and early mitosis.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1652372}. Cytoplasm
CC {ECO:0000269|PubMed:1652372}. Note=Nuclear in G1, cytoplasmic in S, G2
CC and M cell cycle phases.
CC -!- PTM: Cell cycle-dependent phosphorylation of three serine residues
CC prevents SWI5 from entering the nucleus, and it accumulates in the
CC cytoplasm. As a consequence of CDC28 kinase inactivation at the end of
CC anaphase, the three serine residues are dephosphorylated and SWI5
CC enters the nucleus to activate transcription. It is then rapidly
CC degraded. Threonine phosphorylation also seems to occur.
CC -!- PTM: Phosphorylated by PHO85.
CC -!- MISCELLANEOUS: Present with 688 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X06978; CAA30040.1; -; Genomic_DNA.
DR EMBL; Z50046; CAA90369.1; -; Genomic_DNA.
DR EMBL; AY723778; AAU09695.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11989.1; -; Genomic_DNA.
DR PIR; S00342; TWBYS5.
DR RefSeq; NP_010430.1; NM_001180453.1.
DR PDB; 1NCS; NMR; -; A=532-578.
DR PDB; 1ZFD; NMR; -; A=577-608.
DR PDBsum; 1NCS; -.
DR PDBsum; 1ZFD; -.
DR AlphaFoldDB; P08153; -.
DR BMRB; P08153; -.
DR SMR; P08153; -.
DR BioGRID; 32200; 427.
DR DIP; DIP-1461N; -.
DR ELM; P08153; -.
DR IntAct; P08153; 20.
DR MINT; P08153; -.
DR STRING; 4932.YDR146C; -.
DR iPTMnet; P08153; -.
DR MaxQB; P08153; -.
DR PaxDb; P08153; -.
DR PRIDE; P08153; -.
DR EnsemblFungi; YDR146C_mRNA; YDR146C; YDR146C.
DR GeneID; 851724; -.
DR KEGG; sce:YDR146C; -.
DR SGD; S000002553; SWI5.
DR VEuPathDB; FungiDB:YDR146C; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000176710; -.
DR HOGENOM; CLU_021006_0_0_1; -.
DR InParanoid; P08153; -.
DR OMA; GQIVFKM; -.
DR BioCyc; YEAST:G3O-29743-MON; -.
DR EvolutionaryTrace; P08153; -.
DR PRO; PR:P08153; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P08153; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IMP:SGD.
DR GO; GO:0036033; F:mediator complex binding; IMP:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0031496; P:positive regulation of mating type switching; IMP:SGD.
DR GO; GO:0007074; P:positive regulation of transcription involved in exit from mitosis, from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:SGD.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..709
FT /note="Transcriptional factor SWI5"
FT /id="PRO_0000046855"
FT ZN_FING 550..574
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 580..604
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 609..632
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 647..659
FT /note="A.T hook"
FT REGION 245..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 635..659
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 657..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 339
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 522
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:1652372,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 646
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:1652372,
FT ECO:0007744|PubMed:17287358"
FT MOD_RES 664
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:1652372"
FT MUTAGEN 522
FT /note="S->A: Constitutive nuclear entry; when associated
FT with A-646 and A-664."
FT /evidence="ECO:0000269|PubMed:1652372"
FT MUTAGEN 646
FT /note="S->A: Constitutive nuclear entry; when associated
FT with A-522 and A-664."
FT /evidence="ECO:0000269|PubMed:1652372"
FT MUTAGEN 664
FT /note="S->A: Constitutive nuclear entry; when associated
FT with A-522 and A-646."
FT /evidence="ECO:0000269|PubMed:1652372"
FT CONFLICT 514
FT /note="E -> K (in Ref. 4; AAU09695)"
FT /evidence="ECO:0000305"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:1NCS"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:1NCS"
FT TURN 546..548
FT /evidence="ECO:0007829|PDB:1NCS"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:1NCS"
FT STRAND 563..566
FT /evidence="ECO:0007829|PDB:1NCS"
FT HELIX 567..574
FT /evidence="ECO:0007829|PDB:1NCS"
FT TURN 575..577
FT /evidence="ECO:0007829|PDB:1NCS"
FT STRAND 591..594
FT /evidence="ECO:0007829|PDB:1ZFD"
FT HELIX 595..601
FT /evidence="ECO:0007829|PDB:1ZFD"
FT HELIX 602..604
FT /evidence="ECO:0007829|PDB:1ZFD"
SQ SEQUENCE 709 AA; 79775 MW; BEF5ED5BFB6E30F6 CRC64;
MDTSNSWFDA SKVQSLNFDL QTNSYYSNAR GSDPSSYAIE GEYKTLATDD LGNILNLNYG
ETNEVIMNEI NDLNLPLGPL SDEKSVKVST FSELIGNDWQ SMNFDLENNS REVTLNATSL
LNENRLNQDS GMTVYQKTMS DKPHDEKKIS MADNLLSTIN KSEINKGFDR NLGELLLQQQ
QELREQLRAQ QEANKKLELE LKQTQYKQQQ LQATLENSDG PQFLSPKRKI SPASENVEDV
YANSLSPMIS PPMSNTSFTG SPSRRNNRQK YCLQRKNSSG TVGPLCFQEL NEGFNDSLIS
PKKIRSNPNE NLSSKTKFIT PFTPKSRVSS ATSNSANITP NNLRLDFKIN VEDQESEYSE
KPLGLGIELL GKPGPSPTKS VSLKSASVDI MPTIPGSVNN TPSVNKVSLS SSYIDQYTPR
GKQLHFSSIS ENALGINAAT PHLKPPSQQA RHREGVFNDL DPNVLTKNTD NEGDDNEENE
PESRFVISET PSPVLKSQSK YEGRSPQFGT HIKEINTYTT NSPSKITRKL TTLPRGSIDK
YVKEMPDKTF ECLFPGCTKT FKRRYNIRSH IQTHLEDRPY SCDHPGCDKA FVRNHDLIRH
KKSHQEKAYA CPCGKKFNRE DALVVHRSRM ICSGGKKYEN VVIKRSPRKR GRPRKDGTSS
VSSSPIKENI NKDHNGQLMF KLEDQLRRER SYDGNGTGIM VSPMKTNQR
