SPT3_YEAST
ID SPT3_YEAST Reviewed; 337 AA.
AC P06844; D6VT26; Q70DE7; Q70DE9; Q70DF1; Q70DF2;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Protein SPT3;
DE AltName: Full=Positive regulator of Ty transcription;
GN Name=SPT3; OrderedLocusNames=YDR392W; ORFNames=D9509.12;
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=3020500; DOI=10.1093/nar/14.17.6885;
RA Winston F., Minehart P.L.;
RT "Analysis of the yeast SPT3 gene and identification of its product, a
RT positive regulator of Ty transcription.";
RL Nucleic Acids Res. 14:6885-6900(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-76; ASN-93; SER-120;
RP ILE-134 AND LYS-318.
RC STRAIN=CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556,
RC CLIB 630, CLIB 95, K1, R12, R13, Sigma 1278B, YIIc12, and YIIc17;
RX PubMed=15087486; DOI=10.1093/nar/gkh529;
RA Leh-Louis V., Wirth B., Despons L., Wain-Hobson S., Potier S.,
RA Souciet J.-L.;
RT "Differential evolution of the Saccharomyces cerevisiae DUP240 paralogs and
RT implication of recombination in phylogeny.";
RL Nucleic Acids Res. 32:2069-2078(2004).
RN [3]
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 [4]
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 [5]
RP IDENTIFICATION IN THE SAGA COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=9674426; DOI=10.1016/s0092-8674(00)81220-9;
RA Grant P.A., Schieltz D., Pray-Grant M.G., Steger D.J., Reese J.C.,
RA Yates J.R. III, Workman J.L.;
RT "A subset of TAF(II)s are integral components of the SAGA complex required
RT for nucleosome acetylation and transcriptional stimulation.";
RL Cell 94:45-53(1998).
RN [6]
RP FUNCTION IN SAGA TRANSCRIPTIONAL ACTIVATION.
RX PubMed=10580001; DOI=10.1101/gad.13.22.2940;
RA Dudley A.M., Rougeulle C., Winston F.;
RT "The Spt components of SAGA facilitate TBP binding to a promoter at a post-
RT activator-binding step in vivo.";
RL Genes Dev. 13:2940-2945(1999).
RN [7]
RP FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX.
RX PubMed=10026213; DOI=10.1074/jbc.274.9.5895;
RA Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., Workman J.L.;
RT "Expanded lysine acetylation specificity of Gcn5 in native complexes.";
RL J. Biol. Chem. 274:5895-5900(1999).
RN [8]
RP FUNCTION IN SAGA TRANSCRIPTIONAL INHIBITION.
RX PubMed=10611242; DOI=10.1128/mcb.20.2.634-647.2000;
RA Belotserkovskaya R., Sterner D.E., Deng M., Sayre M.H., Lieberman P.M.,
RA Berger S.L.;
RT "Inhibition of TATA-binding protein function by SAGA subunits Spt3 and Spt8
RT at Gcn4-activated promoters.";
RL Mol. Cell. Biol. 20:634-647(2000).
RN [9]
RP FUNCTION IN SAGA TRANSCRIPTIONAL ACTIVATION.
RX PubMed=11485989; DOI=10.1101/gad.911501;
RA Larschan E., Winston F.;
RT "The S. cerevisiae SAGA complex functions in vivo as a coactivator for
RT transcriptional activation by Gal4.";
RL Genes Dev. 15:1946-1956(2001).
RN [10]
RP FUNCTION IN SAGA TRANSCRIPTIONAL ACTIVATION.
RX PubMed=12370284; DOI=10.1128/mcb.22.21.7365-7371.2002;
RA Bhaumik S.R., Green M.R.;
RT "Differential requirement of SAGA components for recruitment of TATA-box-
RT binding protein to promoters in vivo.";
RL Mol. Cell. Biol. 22:7365-7371(2002).
RN [11]
RP IDENTIFICATION IN THE SLIK COMPLEX.
RX PubMed=12446794; DOI=10.1128/mcb.22.24.8774-8786.2002;
RA Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L.,
RA Cook R.G., Workman J.L., Yates J.R. III, Grant P.A.;
RT "The novel SLIK histone acetyltransferase complex functions in the yeast
RT retrograde response pathway.";
RL Mol. Cell. Biol. 22:8774-8786(2002).
RN [12]
RP IDENTIFICATION IN THE SALSA COMPLEX.
RX PubMed=12186975; DOI=10.1073/pnas.182021199;
RA Sterner D.E., Belotserkovskaya R., Berger S.L.;
RT "SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates
RT with activated transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11622-11627(2002).
RN [13]
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 [14]
RP IDENTIFICATION IN THE SLIK COMPLEX.
RX PubMed=15647753; DOI=10.1038/nature03242;
RA Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A.;
RT "Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-
RT dependent acetylation.";
RL Nature 433:434-438(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, 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).
RN [16]
RP 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
RX PubMed=15260971; DOI=10.1016/j.molcel.2004.06.005;
RA Wu P.Y., Ruhlmann C., Winston F., Schultz P.;
RT "Molecular architecture of the S. cerevisiae SAGA complex.";
RL Mol. Cell 15:199-208(2004).
CC -!- FUNCTION: Functions as component of the transcription regulatory
CC histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is
CC involved in RNA polymerase II-dependent transcriptional regulation of
CC approximately 10% of yeast genes. At the promoters, SAGA is required
CC for recruitment of the basal transcription machinery. It influences RNA
CC polymerase II transcriptional activity through different activities
CC such as TBP interaction (SPT3, SPT8 and SPT20) and promoter
CC selectivity, interaction with transcription activators (GCN5, ADA2,
CC ADA3 and TRA1), and chromatin modification through histone acetylation
CC (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone
CC H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA
CC interacts with DNA via upstream activating sequences (UASs). SALSA, an
CC altered form of SAGA, may be involved in positive transcriptional
CC regulation. SPT3 is required for recruitment of TATA-binding protein
CC (TBP) to SAGA-dependent promoters. During SAGA-mediated transcriptional
CC inhibition, SPT3 and SPT8 prevent binding of TBP to the TATA box. SLIK
CC is proposed to have partly overlapping functions with SAGA. It
CC preferentially acetylates methylated histone H3, at least after
CC activation at the GAL1-10 locus. SPT factors 3, 7 and 8 are required
CC for the initiation of Ty transcription from the delta promoter. SPT3
CC regulates Ty1 as well as the mating factor genes.
CC {ECO:0000269|PubMed:10026213, ECO:0000269|PubMed:10580001,
CC ECO:0000269|PubMed:10611242, ECO:0000269|PubMed:11485989,
CC ECO:0000269|PubMed:12370284}.
CC -!- SUBUNIT: Component of the 1.8 MDa SAGA complex, which consists of at
CC least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12,
CC TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and
CC SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2
CC copies. SAGA is built of 5 distinct domains with specialized functions.
CC Domain I (containing TRA1) probably represents the activator
CC interaction surface. Domain II (containing TAF5 and TAF6, and probably
CC TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and
CC ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing
CC HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily
CC an architectural role. Domain III also harbors the HAT activity. Domain
CC V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-
CC interacting module, which may be associated transiently with SAGA. SPT3
CC interacts directly with TBP (TATA-binding protein). Component of the
CC SALSA complex, which consists of at least TRA1, SPT7 (C-terminal
CC truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and
CC SPT3. Component of the SLIK complex, which consists of at least TRA1,
CC CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5,
CC ADA2, SPT3, SGF29, TAF10 and TAF9. {ECO:0000269|PubMed:12186975,
CC ECO:0000269|PubMed:12446794, ECO:0000269|PubMed:15647753,
CC ECO:0000269|PubMed:9674426}.
CC -!- INTERACTION:
CC P06844; Q12060: HFI1; NbExp=9; IntAct=EBI-17921, EBI-8287;
CC P06844; P50875: SPT20; NbExp=9; IntAct=EBI-17921, EBI-17751;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 1710 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SPT3 family. {ECO:0000305}.
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DR EMBL; X04383; CAA27970.1; -; Genomic_DNA.
DR EMBL; AJ585583; CAE52103.1; -; Genomic_DNA.
DR EMBL; AJ585584; CAE52104.1; -; Genomic_DNA.
DR EMBL; AJ585585; CAE52105.1; -; Genomic_DNA.
DR EMBL; AJ585586; CAE52106.1; -; Genomic_DNA.
DR EMBL; AJ585587; CAE52107.1; -; Genomic_DNA.
DR EMBL; AJ585588; CAE52108.1; -; Genomic_DNA.
DR EMBL; AJ585589; CAE52109.1; -; Genomic_DNA.
DR EMBL; AJ585590; CAE52110.1; -; Genomic_DNA.
DR EMBL; AJ585591; CAE52111.1; -; Genomic_DNA.
DR EMBL; AJ585592; CAE52112.1; -; Genomic_DNA.
DR EMBL; AJ585593; CAE52113.1; -; Genomic_DNA.
DR EMBL; AJ585594; CAE52114.1; -; Genomic_DNA.
DR EMBL; AJ585595; CAE52115.1; -; Genomic_DNA.
DR EMBL; AJ585596; CAE52116.1; -; Genomic_DNA.
DR EMBL; AJ585597; CAE52117.1; -; Genomic_DNA.
DR EMBL; AJ585598; CAE52118.1; -; Genomic_DNA.
DR EMBL; AJ585599; CAE52119.1; -; Genomic_DNA.
DR EMBL; U32274; AAB64834.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12236.1; -; Genomic_DNA.
DR PIR; A24330; A24330.
DR RefSeq; NP_010680.1; NM_001180700.1.
DR PDB; 6T9I; EM; 3.90 A; C=1-337.
DR PDB; 6T9K; EM; 3.30 A; C=1-337.
DR PDBsum; 6T9I; -.
DR PDBsum; 6T9K; -.
DR AlphaFoldDB; P06844; -.
DR SMR; P06844; -.
DR BioGRID; 32454; 512.
DR ComplexPortal; CPX-656; SAGA complex.
DR ComplexPortal; CPX-675; SLIK (SAGA-like) complex.
DR DIP; DIP-2204N; -.
DR IntAct; P06844; 26.
DR MINT; P06844; -.
DR STRING; 4932.YDR392W; -.
DR iPTMnet; P06844; -.
DR MaxQB; P06844; -.
DR PaxDb; P06844; -.
DR PRIDE; P06844; -.
DR EnsemblFungi; YDR392W_mRNA; YDR392W; YDR392W.
DR GeneID; 852001; -.
DR KEGG; sce:YDR392W; -.
DR SGD; S000002800; SPT3.
DR VEuPathDB; FungiDB:YDR392W; -.
DR eggNOG; KOG3902; Eukaryota.
DR GeneTree; ENSGT00390000010738; -.
DR HOGENOM; CLU_038706_1_1_1; -.
DR InParanoid; P06844; -.
DR OMA; QFMFNEQ; -.
DR BioCyc; YEAST:G3O-29940-MON; -.
DR PRO; PR:P06844; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P06844; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000124; C:SAGA complex; IDA:SGD.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IDA:SGD.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0003712; F:transcription coregulator activity; IDA:SGD.
DR GO; GO:0006325; P:chromatin organization; IDA:SGD.
DR GO; GO:0016573; P:histone acetylation; IDA:SGD.
DR GO; GO:0016578; P:histone deubiquitination; IC:ComplexPortal.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IDA:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IDA:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:SGD.
DR CDD; cd07978; TAF13; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR003195; TFIID_TAF13.
DR PANTHER; PTHR11380; PTHR11380; 1.
DR Pfam; PF02269; TFIID-18kDa; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..337
FT /note="Protein SPT3"
FT /id="PRO_0000072166"
FT REGION 92..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT VARIANT 76
FT /note="N -> K (in strain: CLIB 556 and CLIB 630)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 93
FT /note="D -> N (in strain: CLIB 556 and CLIB 630)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 120
FT /note="G -> S (in strain: CLIB 413 haplotype Ha2)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 134
FT /note="V -> I (in strain: R13 haplotype Ha2)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 318
FT /note="R -> K (in strain: YIIc12 haplotype Ha2 and YIIc17)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT HELIX 8..18
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 26..54
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 61..65
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 211..216
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 230..263
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 302..312
FT /evidence="ECO:0007829|PDB:6T9K"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:6T9K"
SQ SEQUENCE 337 AA; 38800 MW; E0F60B61AB155C17 CRC64;
MMDKHKYRVE IQQMMFVSGE INDPPVETTS LIEDIVRGQV IEILLQSNKT AHLRGSRSIL
PEDVIFLIRH DKAKVNRLRT YLSWKDLRKN AKDQDASAGV ASGTGNPGAG GEDDLKKAGG
GEKDEKDGGN MMKVKKSQIK LPWELQFMFN EHPLENNDDN DDMDEDEREA NIVTLKRLKM
ADDRTRNMTK EEYVHWSDCR QASFTFRKNK RFKDWSGISQ LTEGKPHDDV IDILGFLTFE
IVCSLTETAL KIKQREQVLQ TQKDKSQQSS QDNTNFEFAS STLHRKKRLF DGPENVINPL
KPRHIEEAWR VLQTIDMRHR ALTNFKGGRL SSKPIIM
