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 27-MAR-2024, entry version 185.
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; 146.
DR DIP; DIP-1307N; -.
DR ELM; P35210; -.
DR IntAct; P35210; 5.
DR MINT; P35210; -.
DR STRING; 4932.YKL020C; -.
DR iPTMnet; P35210; -.
DR MaxQB; 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 GeneTree; ENSGT00940000156179; -.
DR HOGENOM; CLU_004311_0_0_1; -.
DR InParanoid; P35210; -.
DR OMA; IPNWQLC; -.
DR OrthoDB; 2901153at2759; -.
DR BioCyc; YEAST:G3O-31828-MONOMER; -.
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:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IGI:SGD.
DR CDD; cd00102; IPT; 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 PANTHER; PTHR24148; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 39 HOMOLOG-RELATED; 1.
DR PANTHER; PTHR24148:SF77; IPT_TIG DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF12796; Ank_2; 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 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
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