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Protein

Transcription factor SPT8

Gene

SPT8

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required, directly or indirectly, for TATA-binding protein function at particular promoters. May promote a functional interaction between SPT3 and TATA-binding protein. Functions as a component of the transcription regulatory histone acetylation (HAT) complex SAGA. 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).1 Publication

GO - Molecular functioni

  • TBP-class protein binding Source: SGD
  • transcription cofactor activity Source: SGD

GO - Biological processi

  • chromatin modification Source: SGD
  • histone acetylation Source: SGD
  • negative regulation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-32211-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor SPT8
Gene namesi
Name:SPT8
Ordered Locus Names:YLR055C
ORF Names:L2144
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR055C.
SGDiS000004045. SPT8.

Subcellular locationi

GO - Cellular componenti

  • SAGA complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 602602Transcription factor SPT8PRO_0000051226Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei85 – 851PhosphothreonineCombined sources
Modified residuei108 – 1081PhosphoserineCombined sources
Modified residuei123 – 1231PhosphoserineCombined sources
Modified residuei131 – 1311PhosphoserineCombined sources
Modified residuei451 – 4511PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38915.

PTM databases

iPTMnetiP38915.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
DST1P072732EBI-17964,EBI-19168
HFI1Q1206014EBI-17964,EBI-8287
NGG1P324947EBI-17964,EBI-2192
SPT15P133933EBI-17964,EBI-19129
SPT7P3517714EBI-17964,EBI-17958

GO - Molecular functioni

  • TBP-class protein binding Source: SGD

Protein-protein interaction databases

BioGridi31330. 313 interactions.
DIPiDIP-5805N.
IntActiP38915. 183 interactions.
MINTiMINT-635950.

Structurei

3D structure databases

ProteinModelPortaliP38915.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati173 – 21240WD 1Add
BLAST
Repeati305 – 34642WD 2Add
BLAST
Repeati415 – 45440WD 3Add
BLAST
Repeati506 – 54439WD 4Add
BLAST
Repeati560 – 60041WD 5Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 7676Asp/Glu-rich (highly acidic)Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat SPT8 family.Curated
Contains 5 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

HOGENOMiHOG000173633.
InParanoidiP38915.
KOiK11360.
OMAiHDEGKRI.
OrthoDBiEOG7FJH8N.

Family and domain databases

Gene3Di2.130.10.10. 3 hits.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
SMARTiSM00320. WD40. 4 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 3 hits.
PROSITEiPS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38915-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDEVDDILIN NQVVDDEEDD EEMLSGLEND SKQDLEGNDD GGEDEEDDDD
60 70 80 90 100
DDEDDDDDED EREDDDEQED DDGEDDAARM DKTATPTNEH QHDEQKAAAA
110 120 130 140 150
GAGGAGDSGD AVTKIGSEDV KLSDVDGGVG SREASSSTHE ASANGEVYEY
160 170 180 190 200
YKHMLNAAQI ADSYNIYPTA AIPIQTHVNA LAVSRGLKYL FLGGSDGYIR
210 220 230 240 250
KYDLLNTLEG KLSLTILQKH SLAESIQNAG ILQSYWENEI PQKKSEMKLS
260 270 280 290 300
ANKTDYEPKV SPVHSLEVQS ECLFILSGLQ NGGITMQGVR YMEGSIAHYF
310 320 330 340 350
KGRNGHTQIV NILRLNGQED RFLSGSWDKR LLEWDLQTGD IVNEFKKSRS
360 370 380 390 400
ELSSLEMRPL YSSVDVSGNV NSGKENENAD DDMDSLFGDE DEDEKQDAGN
410 420 430 440 450
EPVETGDGSN GEENKEQISE ESLNIVYDES VFMTSGLNGS VHIWDRRMTQ
460 470 480 490 500
SPALSLERGA GVPPWCLSAC WGVDGDHVYA GRRNACVEQF DLKMPSKPIH
510 520 530 540 550
NLKLPSISGP VSCVKAMPNN KHLLCASRDN IRLYNVEIAV DASNSTTKSS
560 570 580 590 600
KVPFLIVPGH HGGIISNLYL DPTSRFIIST SGNRGWQGNS TDTTLIYDID

LE
Length:602
Mass (Da):66,190
Last modified:February 1, 1995 - v1
Checksum:iDDE88155E7638B46
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M94955 Genomic DNA. Translation: AAA53585.1.
X94607 Genomic DNA. Translation: CAA64302.1.
Z73227 Genomic DNA. Translation: CAA97585.1.
BK006945 Genomic DNA. Translation: DAA09373.1.
PIRiS47898.
RefSeqiNP_013156.1. NM_001181942.1.

Genome annotation databases

EnsemblFungiiYLR055C; YLR055C; YLR055C.
GeneIDi850744.
KEGGisce:YLR055C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M94955 Genomic DNA. Translation: AAA53585.1.
X94607 Genomic DNA. Translation: CAA64302.1.
Z73227 Genomic DNA. Translation: CAA97585.1.
BK006945 Genomic DNA. Translation: DAA09373.1.
PIRiS47898.
RefSeqiNP_013156.1. NM_001181942.1.

3D structure databases

ProteinModelPortaliP38915.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31330. 313 interactions.
DIPiDIP-5805N.
IntActiP38915. 183 interactions.
MINTiMINT-635950.

PTM databases

iPTMnetiP38915.

Proteomic databases

MaxQBiP38915.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR055C; YLR055C; YLR055C.
GeneIDi850744.
KEGGisce:YLR055C.

Organism-specific databases

EuPathDBiFungiDB:YLR055C.
SGDiS000004045. SPT8.

Phylogenomic databases

HOGENOMiHOG000173633.
InParanoidiP38915.
KOiK11360.
OMAiHDEGKRI.
OrthoDBiEOG7FJH8N.

Enzyme and pathway databases

BioCyciYEAST:G3O-32211-MONOMER.

Miscellaneous databases

PROiP38915.

Family and domain databases

Gene3Di2.130.10.10. 3 hits.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
SMARTiSM00320. WD40. 4 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 3 hits.
PROSITEiPS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Saccharomyces cerevisiae SPT8 gene encodes a very acidic protein that is functionally related to SPT3 and TATA-binding protein."
    Eisenmann D.M., Chapon C., Roberts S.M., Dollard C., Winston F.
    Genetics 137:647-657(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation."
    Grant P.A., Schieltz D., Pray-Grant M.G., Steger D.J., Reese J.C., Yates J.R. III, Workman J.L.
    Cell 94:45-53(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SAGA COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "Expanded lysine acetylation specificity of Gcn5 in native complexes."
    Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., Workman J.L.
    J. Biol. Chem. 274:5895-5900(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-123; SER-131 AND SER-451, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Molecular architecture of the S. cerevisiae SAGA complex."
    Wu P.Y., Ruhlmann C., Winston F., Schultz P.
    Mol. Cell 15:199-208(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.

Entry informationi

Entry nameiSPT8_YEAST
AccessioniPrimary (citable) accession number: P38915
Secondary accession number(s): D6VY57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 6, 2016
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 8430 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.