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Protein SPT3 (Positive regulator of Ty transcription)

 SPT3_YEAST              Reviewed;         337 AA.
P06844; D6VT26; Q70DE7; Q70DE9; Q70DF1; Q70DF2;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
31-JAN-2018, entry version 167.
RecName: Full=Protein SPT3;
AltName: Full=Positive regulator of Ty transcription;
Name=SPT3; OrderedLocusNames=YDR392W; ORFNames=D9509.12;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3020500; DOI=10.1093/nar/14.17.6885;
Winston F., Minehart P.L.;
"Analysis of the yeast SPT3 gene and identification of its product, a
positive regulator of Ty transcription.";
Nucleic Acids Res. 14:6885-6900(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-76; ASN-93;
SER-120; ILE-134 AND LYS-318.
STRAIN=CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556,
CLIB 630, CLIB 95, K1, R12, R13, Sigma 1278B, YIIc12, and YIIc17;
PubMed=15087486; DOI=10.1093/nar/gkh529;
Leh-Louis V., Wirth B., Despons L., Wain-Hobson S., Potier S.,
Souciet J.-L.;
"Differential evolution of the Saccharomyces cerevisiae DUP240
paralogs and implication of recombination in phylogeny.";
Nucleic Acids Res. 32:2069-2078(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
IDENTIFICATION IN THE SAGA COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=9674426; DOI=10.1016/S0092-8674(00)81220-9;
Grant P.A., Schieltz D., Pray-Grant M.G., Steger D.J., Reese J.C.,
Yates J.R. III, Workman J.L.;
"A subset of TAF(II)s are integral components of the SAGA complex
required for nucleosome acetylation and transcriptional stimulation.";
Cell 94:45-53(1998).
[6]
FUNCTION IN SAGA TRANSCRIPTIONAL ACTIVATION.
PubMed=10580001; DOI=10.1101/gad.13.22.2940;
Dudley A.M., Rougeulle C., Winston F.;
"The Spt components of SAGA facilitate TBP binding to a promoter at a
post-activator-binding step in vivo.";
Genes Dev. 13:2940-2945(1999).
[7]
FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX.
PubMed=10026213; DOI=10.1074/jbc.274.9.5895;
Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M.,
Workman J.L.;
"Expanded lysine acetylation specificity of Gcn5 in native
complexes.";
J. Biol. Chem. 274:5895-5900(1999).
[8]
FUNCTION IN SAGA TRANSCRIPTIONAL INHIBITION.
PubMed=10611242; DOI=10.1128/MCB.20.2.634-647.2000;
Belotserkovskaya R., Sterner D.E., Deng M., Sayre M.H.,
Lieberman P.M., Berger S.L.;
"Inhibition of TATA-binding protein function by SAGA subunits Spt3 and
Spt8 at Gcn4-activated promoters.";
Mol. Cell. Biol. 20:634-647(2000).
[9]
FUNCTION IN SAGA TRANSCRIPTIONAL ACTIVATION.
PubMed=11485989; DOI=10.1101/gad.911501;
Larschan E., Winston F.;
"The S. cerevisiae SAGA complex functions in vivo as a coactivator for
transcriptional activation by Gal4.";
Genes Dev. 15:1946-1956(2001).
[10]
FUNCTION IN SAGA TRANSCRIPTIONAL ACTIVATION.
PubMed=12370284; DOI=10.1128/MCB.22.21.7365-7371.2002;
Bhaumik S.R., Green M.R.;
"Differential requirement of SAGA components for recruitment of TATA-
box-binding protein to promoters in vivo.";
Mol. Cell. Biol. 22:7365-7371(2002).
[11]
IDENTIFICATION IN THE SLIK COMPLEX.
PubMed=12446794; DOI=10.1128/MCB.22.24.8774-8786.2002;
Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L.,
Cook R.G., Workman J.L., Yates J.R. III, Grant P.A.;
"The novel SLIK histone acetyltransferase complex functions in the
yeast retrograde response pathway.";
Mol. Cell. Biol. 22:8774-8786(2002).
[12]
IDENTIFICATION IN THE SALSA COMPLEX.
PubMed=12186975; DOI=10.1073/pnas.182021199;
Sterner D.E., Belotserkovskaya R., Berger S.L.;
"SALSA, a variant of yeast SAGA, contains truncated Spt7, which
correlates with activated transcription.";
Proc. Natl. Acad. Sci. U.S.A. 99:11622-11627(2002).
[13]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[14]
IDENTIFICATION IN THE SLIK COMPLEX.
PubMed=15647753; DOI=10.1038/nature03242;
Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A.;
"Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-
dependent acetylation.";
Nature 433:434-438(2005).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[16]
3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
PubMed=15260971; DOI=10.1016/j.molcel.2004.06.005;
Wu P.Y., Ruhlmann C., Winston F., Schultz P.;
"Molecular architecture of the S. cerevisiae SAGA complex.";
Mol. Cell 15:199-208(2004).
-!- FUNCTION: Functions as component of the transcription regulatory
histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is
involved in RNA polymerase II-dependent transcriptional regulation
of approximately 10% of yeast genes. At the promoters, SAGA is
required for recruitment of the basal transcription machinery. It
influences RNA polymerase II transcriptional activity through
different activities such as TBP interaction (SPT3, SPT8 and
SPT20) and promoter selectivity, interaction with transcription
activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification
through histone acetylation (GCN5) and deubiquitination (UBP8).
SAGA acetylates nucleosomal histone H3 to some extent (to form
H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via
upstream activating sequences (UASs). SALSA, an altered form of
SAGA, may be involved in positive transcriptional regulation. SPT3
is required for recruitment of TATA-binding protein (TBP) to SAGA-
dependent promoters. During SAGA-mediated transcriptional
inhibition, SPT3 and SPT8 prevent binding of TBP to the TATA box.
SLIK is proposed to have partly overlapping functions with SAGA.
It preferentially acetylates methylated histone H3, at least after
activation at the GAL1-10 locus. SPT factors 3, 7 and 8 are
required for the initiation of Ty transcription from the delta
promoter. SPT3 regulates Ty1 as well as the mating factor genes.
{ECO:0000269|PubMed:10026213, ECO:0000269|PubMed:10580001,
ECO:0000269|PubMed:10611242, ECO:0000269|PubMed:11485989,
ECO:0000269|PubMed:12370284}.
-!- SUBUNIT: Component of the 1.8 MDa SAGA complex, which consists of
at least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8,
TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10,
TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem
to be present in 2 copies. SAGA is built of 5 distinct domains
with specialized functions. Domain I (containing TRA1) probably
represents the activator interaction surface. Domain II
(containing TAF5 and TAF6, and probably TAF9 and TAF10), domain
III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably
ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and
TAF6, and probably TAF9) are believed to play primarily an
architectural role. Domain III also harbors the HAT activity.
Domain V (containing SPT3 and SPT20, and probably SPT8) represents
the TBP-interacting module, which may be associated transiently
with SAGA. SPT3 interacts directly with TBP (TATA-binding
protein). Component of the SALSA complex, which consists of at
least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20,
TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of the SLIK
complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3,
SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29,
TAF10 and TAF9. {ECO:0000269|PubMed:12186975,
ECO:0000269|PubMed:12446794, ECO:0000269|PubMed:15647753,
ECO:0000269|PubMed:9674426}.
-!- INTERACTION:
Q12060:HFI1; NbExp=9; IntAct=EBI-17921, EBI-8287;
P50875:SPT20; NbExp=9; IntAct=EBI-17921, EBI-17751;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- MISCELLANEOUS: Present with 1710 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the SPT3 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X04383; CAA27970.1; -; Genomic_DNA.
EMBL; AJ585583; CAE52103.1; -; Genomic_DNA.
EMBL; AJ585584; CAE52104.1; -; Genomic_DNA.
EMBL; AJ585585; CAE52105.1; -; Genomic_DNA.
EMBL; AJ585586; CAE52106.1; -; Genomic_DNA.
EMBL; AJ585587; CAE52107.1; -; Genomic_DNA.
EMBL; AJ585588; CAE52108.1; -; Genomic_DNA.
EMBL; AJ585589; CAE52109.1; -; Genomic_DNA.
EMBL; AJ585590; CAE52110.1; -; Genomic_DNA.
EMBL; AJ585591; CAE52111.1; -; Genomic_DNA.
EMBL; AJ585592; CAE52112.1; -; Genomic_DNA.
EMBL; AJ585593; CAE52113.1; -; Genomic_DNA.
EMBL; AJ585594; CAE52114.1; -; Genomic_DNA.
EMBL; AJ585595; CAE52115.1; -; Genomic_DNA.
EMBL; AJ585596; CAE52116.1; -; Genomic_DNA.
EMBL; AJ585597; CAE52117.1; -; Genomic_DNA.
EMBL; AJ585598; CAE52118.1; -; Genomic_DNA.
EMBL; AJ585599; CAE52119.1; -; Genomic_DNA.
EMBL; U32274; AAB64834.1; -; Genomic_DNA.
EMBL; BK006938; DAA12236.1; -; Genomic_DNA.
PIR; A24330; A24330.
RefSeq; NP_010680.1; NM_001180700.1.
ProteinModelPortal; P06844; -.
BioGrid; 32454; 481.
DIP; DIP-2204N; -.
IntAct; P06844; 26.
MINT; MINT-2731768; -.
STRING; 4932.YDR392W; -.
iPTMnet; P06844; -.
MaxQB; P06844; -.
PaxDb; P06844; -.
PRIDE; P06844; -.
EnsemblFungi; YDR392W; YDR392W; YDR392W.
GeneID; 852001; -.
KEGG; sce:YDR392W; -.
EuPathDB; FungiDB:YDR392W; -.
SGD; S000002800; SPT3.
GeneTree; ENSGT00390000010738; -.
HOGENOM; HOG000205281; -.
InParanoid; P06844; -.
KO; K11313; -.
OMA; RFREWAQ; -.
OrthoDB; EOG092C3CUK; -.
BioCyc; YEAST:G3O-29940-MONOMER; -.
PRO; PR:P06844; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0000124; C:SAGA complex; IDA:SGD.
GO; GO:0046695; C:SLIK (SAGA-like) complex; IDA:SGD.
GO; GO:0003677; F:DNA binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0003712; F:transcription cofactor activity; IDA:SGD.
GO; GO:0006325; P:chromatin organization; IDA:SGD.
GO; GO:0016573; P:histone acetylation; IDA:SGD.
GO; GO:0001403; P:invasive growth in response to glucose limitation; IDA:SGD.
GO; GO:0007124; P:pseudohyphal growth; IDA:SGD.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IMP:SGD.
CDD; cd07978; TAF13; 1.
InterPro; IPR009072; Histone-fold.
InterPro; IPR003195; TFIID_TAF13.
PANTHER; PTHR11380; PTHR11380; 1.
Pfam; PF02269; TFIID-18kDa; 1.
SUPFAM; SSF47113; SSF47113; 1.
1: Evidence at protein level;
Activator; Complete proteome; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation.
CHAIN 1 337 Protein SPT3.
/FTId=PRO_0000072166.
MOD_RES 270 270 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
VARIANT 76 76 N -> K (in strain: CLIB 556 and CLIB
630). {ECO:0000269|PubMed:15087486}.
VARIANT 93 93 D -> N (in strain: CLIB 556 and CLIB
630). {ECO:0000269|PubMed:15087486}.
VARIANT 120 120 G -> S (in strain: CLIB 413 haplotype
Ha2). {ECO:0000269|PubMed:15087486}.
VARIANT 134 134 V -> I (in strain: R13 haplotype Ha2).
{ECO:0000269|PubMed:15087486}.
VARIANT 318 318 R -> K (in strain: YIIc12 haplotype Ha2
and YIIc17).
{ECO:0000269|PubMed:15087486}.
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


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