ID SPT20_YEAST Reviewed; 604 AA.
AC P50875; D6W1S1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 27-MAR-2024, entry version 179.
DE RecName: Full=Transcription factor SPT20;
GN Name=SPT20; Synonyms=ADA5; OrderedLocusNames=YOL148C;
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].
RC STRAIN=ATCC MYA-3516 / BWG1-7A;
RX PubMed=8649430; DOI=10.1128/mcb.16.6.3197;
RA Marcus G.A., Horiuchi J., Silverman N., Guarente L.;
RT "ADA5/SPT20 links the ADA and SPT genes, which are involved in yeast
RT transcription.";
RL Mol. Cell. Biol. 16:3197-3205(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8649431; DOI=10.1128/mcb.16.6.3206;
RA Roberts S.M., Winston F.;
RT "SPT20/ADA5 encodes a novel protein functionally related to the TATA-
RT binding protein and important for transcription in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 16:3206-3213(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-604.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8553699; DOI=10.1002/yea.320111308;
RA Casamayor A., Aldea M., Casas C., Herrero E., Gamo F.-J., Lafuente M.J.,
RA Gancedo C., Arino J.;
RT "DNA sequence analysis of a 13 kbp fragment of the left arm of yeast
RT chromosome XV containing seven new open reading frames.";
RL Yeast 11:1281-1288(1995).
RN [6]
RP IDENTIFICATION IN THE ADA/GCN5 COMPLEX.
RC STRAIN=ATCC MYA-3516 / BWG1-7A;
RX PubMed=9154821; DOI=10.1128/mcb.17.6.3220;
RA Horiuchi J., Silverman N., Pina B., Marcus G.A., Guarente L.;
RT "ADA1, a novel component of the ADA/GCN5 complex, has broader effects than
RT GCN5, ADA2, or ADA3.";
RL Mol. Cell. Biol. 17:3220-3228(1997).
RN [7]
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 [8]
RP IDENTIFICATION IN A SAGA COMPLEX WITH SPT2; SPT7; SPT8; GCN5; HFI1; ADA2;
RP ADA3 AND TRA1.
RX PubMed=9885573; DOI=10.1016/s1097-2765(00)80300-7;
RA Grant P.A., Schieltz D., Pray-Grant M.G., Yates J.R. III, Workman J.L.;
RT "The ATM-related cofactor Tra1 is a component of the purified SAGA
RT complex.";
RL Mol. Cell 2:863-867(1998).
RN [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-516, AND IDENTIFICATION BY
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446, 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: Transcription regulator. May recruit TATA binding protein
CC (TBP) and possibly other basal factors to bind to the TATA box.
CC Functions as a component of the transcription regulatory histone
CC acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is involved in
CC RNA polymerase II-dependent transcriptional regulation of approximately
CC 10% of yeast genes. At the promoters, SAGA is required for recruitment
CC of the basal transcription machinery. It influences RNA polymerase II
CC transcriptional activity through different activities such as TBP
CC interaction (SPT3, SPT8 and SPT20) and promoter selectivity,
CC interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1),
CC and chromatin modification through histone acetylation (GCN5) and
CC deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some
CC extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts
CC with DNA via upstream activating sequences (UASs). SALSA, an altered
CC form of SAGA, may be involved in positive transcriptional regulation.
CC SLIK 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. {ECO:0000269|PubMed:10026213}.
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. SUS1
CC associates with the SAC3-THP1 complex. Component of the SALSA complex,
CC which consists of at least TRA1, SPT7 (C-terminal truncated form),
CC TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of
CC the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5,
CC ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29,
CC TAF10 and TAF9. Component of the ADA/GCN5 complex that consists of
CC HFI1/ADA1, ADA2, ADA3, SPT20/ADA5 and GCN5 and is probably a subcomplex
CC of SAGA. {ECO:0000269|PubMed:12186975, ECO:0000269|PubMed:12446794,
CC ECO:0000269|PubMed:15647753, ECO:0000269|PubMed:9154821,
CC ECO:0000269|PubMed:9674426, ECO:0000269|PubMed:9885573}.
CC -!- INTERACTION:
CC P50875; Q12060: HFI1; NbExp=13; IntAct=EBI-17751, EBI-8287;
CC P50875; P53165: SGF73; NbExp=7; IntAct=EBI-17751, EBI-23812;
CC P50875; P06844: SPT3; NbExp=9; IntAct=EBI-17751, EBI-17921;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 4150 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SPT20 family. {ECO:0000305}.
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DR EMBL; U43153; AAB07899.1; -; Genomic_DNA.
DR EMBL; U22063; AAB07900.1; -; Genomic_DNA.
DR EMBL; Z74890; CAA99169.1; -; Genomic_DNA.
DR EMBL; Z48239; CAA88279.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10637.1; -; Genomic_DNA.
DR PIR; S58643; S58643.
DR RefSeq; NP_014493.1; NM_001183402.1.
DR PDB; 6T9I; EM; 3.90 A; B=1-604.
DR PDB; 6T9J; EM; 3.40 A; B=1-604.
DR PDB; 6T9K; EM; 3.30 A; B=1-604.
DR PDBsum; 6T9I; -.
DR PDBsum; 6T9J; -.
DR PDBsum; 6T9K; -.
DR AlphaFoldDB; P50875; -.
DR EMDB; EMD-10412; -.
DR EMDB; EMD-10413; -.
DR EMDB; EMD-10414; -.
DR SMR; P50875; -.
DR BioGRID; 34269; 103.
DR ComplexPortal; CPX-656; SAGA complex.
DR ComplexPortal; CPX-675; SLIK (SAGA-like) complex.
DR DIP; DIP-933N; -.
DR IntAct; P50875; 85.
DR MINT; P50875; -.
DR STRING; 4932.YOL148C; -.
DR GlyGen; P50875; 11 sites, 1 O-linked glycan (11 sites).
DR iPTMnet; P50875; -.
DR MaxQB; P50875; -.
DR PaxDb; 4932-YOL148C; -.
DR PeptideAtlas; P50875; -.
DR EnsemblFungi; YOL148C_mRNA; YOL148C; YOL148C.
DR GeneID; 854017; -.
DR KEGG; sce:YOL148C; -.
DR AGR; SGD:S000005508; -.
DR SGD; S000005508; SPT20.
DR VEuPathDB; FungiDB:YOL148C; -.
DR eggNOG; ENOG502QS30; Eukaryota.
DR HOGENOM; CLU_431618_0_0_1; -.
DR InParanoid; P50875; -.
DR OMA; YDHTNTV; -.
DR OrthoDB; 1949466at2759; -.
DR BioCyc; YEAST:G3O-33538-MONOMER; -.
DR BioGRID-ORCS; 854017; 5 hits in 10 CRISPR screens.
DR PRO; PR:P50875; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P50875; Protein.
DR GO; GO:0005634; C:nucleus; NAS:ComplexPortal.
DR GO; GO:0000124; C:SAGA complex; IDA:SGD.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IDA:SGD.
DR GO; GO:0003712; F:transcription coregulator activity; IMP:SGD.
DR GO; GO:0006325; P:chromatin organization; IDA:SGD.
DR GO; GO:0036498; P:IRE1-mediated unfolded protein response; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR InterPro; IPR021950; Spt20.
DR InterPro; IPR046468; Spt20-like_SEP.
DR PANTHER; PTHR13526; TRANSCRIPTION FACTOR SPT20 HOMOLOG; 1.
DR PANTHER; PTHR13526:SF8; TRANSCRIPTION FACTOR SPT20 HOMOLOG; 1.
DR Pfam; PF12090; Spt20_SEP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..604
FT /note="Transcription factor SPT20"
FT /id="PRO_0000072161"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 516
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 293
FT /note="Y -> S (in Ref. 5; CAA88279)"
FT /evidence="ECO:0000305"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:6T9K"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:6T9K"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 279..286
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 289..299
FT /evidence="ECO:0007829|PDB:6T9K"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 307..321
FT /evidence="ECO:0007829|PDB:6T9K"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:6T9K"
FT TURN 391..397
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 404..412
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 476..487
FT /evidence="ECO:0007829|PDB:6T9J"
SQ SEQUENCE 604 AA; 67796 MW; 3D67937B65F9AA6A CRC64;
MSANSPTGND PHVFGIPVNA TPSNMGSPGS PVNVPPPMNP AVANVNHPVM RTNSNSNANE
GTRTLTREQI QQLQQRQRLL LQQRLLEQQR KQQALQNYEA QFYQMLMTLN KRPKRLYNFV
EDADSILKKY EQYLHSFEFH IYENNYKICA PANSRLQQQQ KQPELTSDGL ILTKNNETLK
EFLEYVARGR IPDAIMEVLR DCNIQFYEGN LILQVYDHTN TVDVTPKENK PNLNSSSSPS
NNNSTQDNSK IQQPSEPNSG VANTGANTAN KKASFKRPRV YRTLLKPNDL TTYYDMMSYA
DNARFSDSIY QQFESEILTL TKRNLSLSVP LNPYEHRDML EETAFSEPHW DSEKKSFIHE
HRAESTREGT KGVVGHIEER DEFPQHSSNY EQLMLIMNER TTTITNSTFA VSLTKNAMEI
ASSSSNGVRG ASSSTSNSAS NTRNNSLANG NQVALAAAAA AAAVGSTMGN DNNQFSRLKF
IEQWRINKEK RKQQALSANI NPTPFNARIS MTAPLTPQQQ LLQRQQQALE QQQNGGAMKN
ANKRSGNNAT SNNNNNNNNL DKPKVKRPRK NAKKSESGTP APKKKRMTKK KQSASSTPSS
TTMS
//
