SNT1_YEAST
ID SNT1_YEAST Reviewed; 1226 AA.
AC P25357; D6VR43; Q02397; Q8NIL8;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Probable DNA-binding protein SNT1;
DE AltName: Full=SANT domain-containing protein 1;
GN Name=SNT1; OrderedLocusNames=YCR033W; ORFNames=YCR33W, YCR592;
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=1776366; DOI=10.1002/yea.320070711;
RA Wicksteed B.L., Roberts A.B., Sagliocco F.A., Brown A.J.P.;
RT "The complete sequence of a 7.5 kb region of chromosome III from
RT Saccharomyces cerevisiae that lies between CRY1 and MAT.";
RL Yeast 7:761-772(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1872032; DOI=10.1002/yea.320070411;
RA Jia Y., Slonimski P.P., Herbert C.J.;
RT "The complete sequence of the unit YCR59, situated between CRY1 and MAT,
RT reveals two long open reading frames, which cover 91% of the 10.1 kb
RT segment.";
RL Yeast 7:413-424(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [4]
RP SEQUENCE REVISION.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP IDENTIFICATION IN A COMPLEX WITH SET3; HST1; HOS2; SIF2; CPR1 AND HOS4.
RX PubMed=11711434; DOI=10.1101/gad.207401;
RA Pijnappel W.W.M.P., Schaft D., Roguev A., Shevchenko A., Tekotte H.,
RA Wilm M., Rigaut G., Seraphin B., Aasland R., Stewart A.F.;
RT "The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and
RT Hst1, and is a meiotic-specific repressor of the sporulation gene
RT program.";
RL Genes Dev. 15:2991-3004(2001).
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 [LARGE SCALE ANALYSIS] AT SER-187; SER-395; THR-796 AND
RP SER-1037, AND 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-796, 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).
CC -!- FUNCTION: Part of the Set3C complex, which is required to repress
CC early/middle sporulation genes during meiosis.
CC -!- SUBUNIT: Identified in a Set3C complex with SET3, HST1, HOS2, SIF2,
CC CPR1 and HOS4. {ECO:0000269|PubMed:11711434}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 396 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; S78624; AAB21259.1; -; Genomic_DNA.
DR EMBL; X59075; CAA41799.1; -; Genomic_DNA.
DR EMBL; X59720; CAC42983.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07512.1; -; Genomic_DNA.
DR PIR; S15053; S15053.
DR RefSeq; NP_009962.2; NM_001178747.1.
DR AlphaFoldDB; P25357; -.
DR SMR; P25357; -.
DR BioGRID; 31016; 676.
DR ComplexPortal; CPX-1342; SET3C histone deacetylase complex.
DR DIP; DIP-2082N; -.
DR IntAct; P25357; 14.
DR MINT; P25357; -.
DR STRING; 4932.YCR033W; -.
DR iPTMnet; P25357; -.
DR MaxQB; P25357; -.
DR PaxDb; P25357; -.
DR PRIDE; P25357; -.
DR EnsemblFungi; YCR033W_mRNA; YCR033W; YCR033W.
DR GeneID; 850399; -.
DR KEGG; sce:YCR033W; -.
DR SGD; S000000629; SNT1.
DR VEuPathDB; FungiDB:YCR033W; -.
DR eggNOG; KOG1878; Eukaryota.
DR GeneTree; ENSGT00940000175552; -.
DR HOGENOM; CLU_004864_0_0_1; -.
DR InParanoid; P25357; -.
DR OMA; YKHHQLA; -.
DR BioCyc; YEAST:G3O-29347-MON; -.
DR Reactome; R-SCE-3214815; HDACs deacetylate histones.
DR PRO; PR:P25357; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25357; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; HDA:SGD.
DR GO; GO:0034967; C:Set3 complex; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IC:ComplexPortal.
DR GO; GO:0009267; P:cellular response to starvation; IC:ComplexPortal.
DR GO; GO:0016575; P:histone deacetylation; IDA:UniProtKB.
DR GO; GO:0045835; P:negative regulation of meiotic nuclear division; IDA:UniProtKB.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:SGD.
DR CDD; cd00167; SANT; 2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS51293; SANT; 1.
PE 1: Evidence at protein level;
KW Coiled coil; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..1226
FT /note="Probable DNA-binding protein SNT1"
FT /id="PRO_0000197122"
FT DOMAIN 668..720
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 884..938
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 911..934
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 539..591
FT /evidence="ECO:0000255"
FT COMPBIAS 22..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 796
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1037
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 305
FT /note="A -> T (in Ref. 2; CAA41799)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="S -> N (in Ref. 2; CAA41799)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="Q -> H (in Ref. 2; CAA41799)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="V -> A (in Ref. 2; CAA41799)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="N -> D (in Ref. 2; CAA41799)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="E -> K (in Ref. 2; CAA41799)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="L -> V (in Ref. 1; AAB21259)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="H -> Y (in Ref. 2; CAA41799)"
FT /evidence="ECO:0000305"
FT CONFLICT 766
FT /note="E -> D (in Ref. 2; CAA41799)"
FT /evidence="ECO:0000305"
FT CONFLICT 806
FT /note="Q -> K (in Ref. 2; CAA41799)"
FT /evidence="ECO:0000305"
FT CONFLICT 831
FT /note="V -> I (in Ref. 2; CAA41799)"
FT /evidence="ECO:0000305"
FT CONFLICT 846
FT /note="G -> E (in Ref. 2; CAA41799)"
FT /evidence="ECO:0000305"
FT CONFLICT 851
FT /note="D -> A (in Ref. 2; CAA41799)"
FT /evidence="ECO:0000305"
FT CONFLICT 855..857
FT /note="AVQ -> GVR (in Ref. 2; CAA41799)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1226 AA; 138397 MW; 70AE6622227088EB CRC64;
MGYPPPTRRL GDKKRYHYSN NPNRRHPSAV YSKNSFPKSS NNGFVSSPTA DNSTNPSVTP
STASVPLPTA APGSTFGIEA PRPSRYDPSS VSRPSSSSYS STRKIGSRYN PDVERSSSTT
SSTPESMNTS TITHTNTDIG NSRYSRKTMS RYNPQSTSST NVTHFPSALS NAPPFYVANG
SSRRPRSMDD YSPDVTNKLE TNNVSSVNNN SPHSYYSRSN KWRSIGTPSR PPFDNHVGNM
TTTSNTNSIH QREPFWKANS TTILKSTHSQ SSPSLHTKKF HDANKLDKPE ASVKVETPSK
DETKAISYHD NNFPPRKSVS KPNAPLEPDN IKVGEEDALG KKEVHKSGRE IAKEHPTPVK
MKEHDELEAR AKKVSKINID GKQDEIWTTA KTVASAVEVS KESQKELTRS VERKESPEIR
DYERAYDPKA LKTDVTKLTV DNDNKSYEEP LEKVEGCIFP LPKAETRLWE LKNQKRNKII
SEQKYLLKKA IRNFSEYPFY AQNKLIHQQA TGLILTKIIS KIKKEEHLKK INLKHDYFDL
QKKYEKECEI LTKLSENLRK EEIENKRKEH ELMEQKRREE GIETEKEKSL RHPSSSSSSR
RRNRADFVDD AEMENVLLQI DPNYKHYQAA ATIPPLILDP IRKHSYKFCD VNNLVTDKKL
WASRILKDAS DNFTDHEHSL FLEGYLIHPK KFGKISHYMG GLRSPEECVL HYYRTKKTVN
YKQLLIDKNK KRKMSAAAKR RKRKERSNDE EVEVDESKEE STNTIEKEEK SENNAEENVQ
PVLVQGSEVK GDPLGTPEKV ENMIEQRGEE FAGELENAER VNDLKRAHDE VGEESNKSSV
IETNNGVQIM DPKGAVQNGY YPEETKELDF SLENALQRKK HKSAPEHKTS YWSVRESQLF
PELLKEFGSQ WSLISEKLGT KSTTMVRNYY QRNAARNGWK LLVDETDLKR DGTSSESVQQ
SQILIQPERP NINAYSNIPP QQRPALGYFV GQPTHGHNTS ISSIDGSIRP FGPDFHRDTF
SKISAPLTTL PPPRLPSIQF PRSEMAEPTV TDLRNRPLDH IDTLADAASS VTNNQNFSNE
RNAIDIGRKS TTISNLLNNS DRSMKSSFQS ASRHEAQLED TPSMNNIVVQ EIKPNITTPR
SSSISALLNP VNGNGQSNPD GRPLLPFQHA ISQGTPTFPL PAPRTSPISR APPKFNFSND
PLAALAAVAS APDAMSSFLS KKENNN
