ID   SPT23_YEAST             Reviewed;        1082 AA.
AC   P35210; D6VXR5;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   02-SEP-2026, entry version 195.
DE   RecName: Full=Protein SPT23;
GN   Name=SPT23; OrderedLocusNames=YKL020C;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 136-752.
RX   PubMed=8203154; DOI=10.1002/yea.320100108;
RA   Burkett T.J., Garfinkel D.J.;
RT   "Molecular characterization of the SPT23 gene: a dosage-dependent
RT   suppressor of Ty-induced promoter mutations from Saccharomyces
RT   cerevisiae.";
RL   Yeast 10:81-92(1994).
RN   [4]
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468, 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: Dosage-dependent suppressor of Ty-induced promoter mutations.
CC       May exert its suppression effect through protein-protein interactions
CC       since does not present any of the motifs generally found in
CC       transcriptional activators or DNA binding proteins.
CC   -!- MISCELLANEOUS: Present with 432 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA20575.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; Z28020; CAA81855.1; -; Genomic_DNA.
DR   EMBL; L24760; AAA20575.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BK006944; DAA09135.1; -; Genomic_DNA.
DR   PIR; S37837; S37837.
DR   RefSeq; NP_012905.1; NM_001179586.1.
DR   AlphaFoldDB; P35210; -.
DR   SMR; P35210; -.
DR   BioGRID; 34111; 147.
DR   DIP; DIP-1307N; -.
DR   ELM; P35210; -.
DR   FunCoup; P35210; 1730.
DR   IntAct; P35210; 6.
DR   MINT; P35210; -.
DR   STRING; 4932.YKL020C; -.
DR   iPTMnet; P35210; -.
DR   PaxDb; 4932-YKL020C; -.
DR   PeptideAtlas; P35210; -.
DR   EnsemblFungi; YKL020C_mRNA; YKL020C; YKL020C.
DR   GeneID; 853848; -.
DR   KEGG; sce:YKL020C; -.
DR   AGR; SGD:S000001503; -.
DR   SGD; S000001503; SPT23.
DR   VEuPathDB; FungiDB:YKL020C; -.
DR   eggNOG; KOG3836; Eukaryota.
DR   HOGENOM; CLU_004311_0_0_1; -.
DR   InParanoid; P35210; -.
DR   OMA; IPNWQLC; -.
DR   OrthoDB; 71307at2759; -.
DR   BioCyc; YEAST:G3O-31828-MONOMER; -.
DR   Reactome; R-SCE-8948751; Regulation of PTEN stability and activity.
DR   BioGRID-ORCS; 853848; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P35210; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P35210; protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0070417; P:cellular response to cold; IGI:SGD.
DR   GO; GO:0055089; P:fatty acid homeostasis; IDA:SGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:2001280; P:positive regulation of unsaturated fatty acid biosynthetic process; IDA:SGD.
DR   GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IGI:SGD.
DR   CDD; cd00102; IPT; 1.
DR   FunFam; 2.60.40.10:FF:001880; Mga2p; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_dom.
DR   InterPro; IPR057962; SPT23_MGA2_DBD.
DR   PANTHER; PTHR24124; ANKYRIN REPEAT FAMILY A; 1.
DR   PANTHER; PTHR24124:SF8; OCA DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF25603; SPT23_MGA2_DBD; 1.
DR   Pfam; PF01833; TIG; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00429; IPT; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
PE   1: Evidence at protein level;
KW   ANK repeat; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..1082
FT                   /note="Protein SPT23"
FT                   /id="PRO_0000067076"
FT   DOMAIN          508..585
FT                   /note="IPT/TIG"
FT   REPEAT          709..738
FT                   /note="ANK 1"
FT   REPEAT          742..771
FT                   /note="ANK 2"
FT   REGION          315..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          376..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..328
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..346
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..391
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..416
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         468
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        715
FT                   /note="H -> P (in Ref. 3; AAA20575)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1082 AA;  121338 MW;  620C688ECC0ECBD7 CRC64;
     MMSGTGNVSS MLHSYSANIQ HNDGSPDLDL LESELLDIAL LNSGSSLQDP GLLSLNQEKM
     ITAGTTTPGK EDEGELRDDI ASLQGLLDRH VQFGRKLPLR TPYANPLDFI NINPQSLPLS
     LEIIGLPKVS RVETQMKLSF RIRNAHARKN FFIHLPSDCI AKDKFFTSSD DPTNLTIPNR
     DINERTLFLD AFLLCASNNN SNNFKQTYVC NRCINREKRR ASRRKSGLND NSIWQNNENK
     RAIIFNSKQL FIISNNGLSG NSNCINFDLP TRIVCYCRHH KATNGFVVLF LLRDHNGDIL
     AKTITDPIMI MDKKNASNTT TPTSTSNAQV SPMTNDTRSF SSPQSDLNFP SEFPLPSNSK
     NFVISTNCML DSNCNNNNND NDNKNNIKTN TAMMNNNRHF PSPNSSSEDS NHSFSDIHFS
     NNNDNNLHRS LDSWSSTGFN SSSNPALTTL TSDFSAASAR HTGKRQRSVN EPFMSTPNTF
     SRLPQKFIDS SKDISNHNSV PVALNNKPSI QRVIPAQGSI NGGIEVTLLG SKFKQGLIIK
     FGENIALSSQ CWNESTMVTY LPPSSKPGPV LVTIVDPSET SMRNNSNSSV STSNSTNDIL
     HLNKYTGEKA IFTYVDDTDR QLIELALQIV GLKMNGKLED ARNIAKRIVG SDSSPSNNNA
     GLHSQNSSLN SYTNMMRNIN DEQLITEVIK SFKRNNNLST VNLSMCDVRG RTLLHLAAFN
     NWYSLVSLLI KYGSHLNDQD LFGFTPLHMA CINGDLRIIR LLLECNVNIM KKTRNGFIAK
     QFFLMNYTVN KTRYSNYETS LFDDILTRLT KNTTGSSDTQ PFERNVSQSS FNSSLFDDDD
     ADHDYVQERK YLLADSAALA PEQSNCNDNT SFSILDSDSG YDISDCESSS DEIALEFFNT
     HKIKDFSSKP NEIPKTTKTS IEPDGSLWNR MLTRLNDELP KYEDLFPKKP KNWELGSKSV
     EIGPDNSAQM TVDDSQTSSE DDELEALQVG FNTIFSKKQN FQNDKMLLFF WIPLTLVLLL
     CFTLSNLGKD DDMFHNLSKI VQEYLRIGLA KVLLGNERMK TSFKMQLSKF QNNNILNDMR
     VN
//