SPT8_YEAST
ID SPT8_YEAST Reviewed; 602 AA.
AC P38915; D6VY57;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Transcription factor SPT8;
GN Name=SPT8; OrderedLocusNames=YLR055C; ORFNames=L2144;
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 204508 / S288c;
RX PubMed=8088510; DOI=10.1093/genetics/137.3.647;
RA Eisenmann D.M., Chapon C., Roberts S.M., Dollard C., Winston F.;
RT "The Saccharomyces cerevisiae SPT8 gene encodes a very acidic protein that
RT is functionally related to SPT3 and TATA-binding protein.";
RL Genetics 137:647-657(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-85, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-123; SER-131 AND
RP SER-451, AND IDENTIFICATION BY 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 [9]
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: Required, directly or indirectly, for TATA-binding protein
CC function at particular promoters. May promote a functional interaction
CC between SPT3 and TATA-binding protein. Functions as a component of the
CC transcription regulatory histone acetylation (HAT) complex SAGA. SAGA
CC is involved in RNA polymerase II-dependent transcriptional regulation
CC of 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).
CC {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.
CC {ECO:0000269|PubMed:9674426}.
CC -!- INTERACTION:
CC P38915; P07273: DST1; NbExp=2; IntAct=EBI-17964, EBI-19168;
CC P38915; Q12060: HFI1; NbExp=14; IntAct=EBI-17964, EBI-8287;
CC P38915; P32494: NGG1; NbExp=7; IntAct=EBI-17964, EBI-2192;
CC P38915; P13393: SPT15; NbExp=3; IntAct=EBI-17964, EBI-19129;
CC P38915; P35177: SPT7; NbExp=13; IntAct=EBI-17964, EBI-17958;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 8430 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat SPT8 family. {ECO:0000305}.
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DR EMBL; M94955; AAA53585.1; -; Genomic_DNA.
DR EMBL; X94607; CAA64302.1; -; Genomic_DNA.
DR EMBL; Z73227; CAA97585.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09373.1; -; Genomic_DNA.
DR PIR; S47898; S47898.
DR RefSeq; NP_013156.1; NM_001181942.1.
DR AlphaFoldDB; P38915; -.
DR BioGRID; 31330; 417.
DR ComplexPortal; CPX-656; SAGA complex.
DR DIP; DIP-5805N; -.
DR IntAct; P38915; 184.
DR MINT; P38915; -.
DR STRING; 4932.YLR055C; -.
DR iPTMnet; P38915; -.
DR MaxQB; P38915; -.
DR PaxDb; P38915; -.
DR PRIDE; P38915; -.
DR EnsemblFungi; YLR055C_mRNA; YLR055C; YLR055C.
DR GeneID; 850744; -.
DR KEGG; sce:YLR055C; -.
DR SGD; S000004045; SPT8.
DR VEuPathDB; FungiDB:YLR055C; -.
DR eggNOG; ENOG502QS8F; Eukaryota.
DR HOGENOM; CLU_010934_2_1_1; -.
DR InParanoid; P38915; -.
DR OMA; IWDRRQP; -.
DR BioCyc; YEAST:G3O-32211-MON; -.
DR PRO; PR:P38915; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P38915; protein.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000124; C:SAGA complex; IDA:SGD.
DR GO; GO:0017025; F:TBP-class protein binding; IDA:SGD.
DR GO; GO:0003712; F:transcription coregulator activity; IMP: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:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; WD repeat.
FT CHAIN 1..602
FT /note="Transcription factor SPT8"
FT /id="PRO_0000051226"
FT REPEAT 173..212
FT /note="WD 1"
FT REPEAT 305..346
FT /note="WD 2"
FT REPEAT 415..454
FT /note="WD 3"
FT REPEAT 506..544
FT /note="WD 4"
FT REPEAT 560..600
FT /note="WD 5"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..76
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..398
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 602 AA; 66190 MW; DDE88155E7638B46 CRC64;
MDEVDDILIN NQVVDDEEDD EEMLSGLEND SKQDLEGNDD GGEDEEDDDD DDEDDDDDED
EREDDDEQED DDGEDDAARM DKTATPTNEH QHDEQKAAAA GAGGAGDSGD AVTKIGSEDV
KLSDVDGGVG SREASSSTHE ASANGEVYEY YKHMLNAAQI ADSYNIYPTA AIPIQTHVNA
LAVSRGLKYL FLGGSDGYIR KYDLLNTLEG KLSLTILQKH SLAESIQNAG ILQSYWENEI
PQKKSEMKLS ANKTDYEPKV SPVHSLEVQS ECLFILSGLQ NGGITMQGVR YMEGSIAHYF
KGRNGHTQIV NILRLNGQED RFLSGSWDKR LLEWDLQTGD IVNEFKKSRS ELSSLEMRPL
YSSVDVSGNV NSGKENENAD DDMDSLFGDE DEDEKQDAGN EPVETGDGSN GEENKEQISE
ESLNIVYDES VFMTSGLNGS VHIWDRRMTQ SPALSLERGA GVPPWCLSAC WGVDGDHVYA
GRRNACVEQF DLKMPSKPIH NLKLPSISGP VSCVKAMPNN KHLLCASRDN IRLYNVEIAV
DASNSTTKSS KVPFLIVPGH HGGIISNLYL DPTSRFIIST SGNRGWQGNS TDTTLIYDID
LE
