Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Transcription factor SPN1

Gene

SPN1

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

Transcription factor involved in RNA polymerase II transcription regulation. May function in both SPT15/TBP post-recruitment and recruitment steps of transcription.2 Publications

GO - Molecular functioni

GO - Biological processi

  • chromatin maintenance Source: SGD
  • poly(A)+ mRNA export from nucleus Source: SGD
  • regulation of nucleosome density Source: SGD
  • regulation of transcription elongation from RNA polymerase II promoter Source: SGD
  • 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-34269-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor SPN1
Alternative name(s):
Interacts with SPT6 protein 1
Suppresses postrecruitment functions protein 1
Gene namesi
Name:SPN1
Synonyms:IWS1
Ordered Locus Names:YPR133C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR133C.
SGDiS000006337. SPN1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi192 – 1921K → N: Suppresses postrecruitment-defective SPT15/TBP alleles. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 410410Transcription factor SPN1PRO_0000083366Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151PhosphothreonineCombined sources
Modified residuei23 – 231Phosphoserine; by ATM or ATRCombined sources
Modified residuei40 – 401PhosphoserineCombined sources
Modified residuei85 – 851PhosphoserineCombined sources
Modified residuei86 – 861PhosphothreonineCombined sources
Modified residuei89 – 891PhosphoserineCombined sources1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ06505.

PTM databases

iPTMnetiQ06505.

Interactioni

Subunit structurei

Interacts with ABD1, RBP1, SPT5 and SPT6.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SPT6P236157EBI-32596,EBI-17947

Protein-protein interaction databases

BioGridi36299. 86 interactions.
DIPiDIP-3823N.
IntActiQ06505. 10 interactions.
MINTiMINT-529538.

Structurei

Secondary structure

1
410
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi150 – 18233Combined sources
Helixi191 – 20313Combined sources
Helixi206 – 2083Combined sources
Helixi209 – 2146Combined sources
Helixi217 – 2259Combined sources
Helixi236 – 24712Combined sources
Helixi253 – 2597Combined sources
Helixi261 – 27010Combined sources
Beta strandi272 – 2743Combined sources
Helixi276 – 28914Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NFQX-ray1.85A/B141-310[»]
3O8ZX-ray2.15A148-295[»]
3OAKX-ray2.15A/B148-292[»]
ProteinModelPortaliQ06505.
SMRiQ06505. Positions 148-295.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06505.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini219 – 29678TFIIS N-terminalPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the IWS1 family.Curated
Contains 1 TFIIS N-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00720000108834.
HOGENOMiHOG000001004.
InParanoidiQ06505.
KOiK17498.
OMAiIGASDNY.
OrthoDBiEOG7N0CHQ.

Family and domain databases

Gene3Di1.20.930.10. 1 hit.
InterProiIPR017923. TFIIS_N.
[Graphical view]
PfamiPF08711. Med26. 1 hit.
[Graphical view]
PROSITEiPS51319. TFIIS_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06505-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTADQEQPK VVEATPEDGT ASSQKSTINA ENENTKQNQS MEPQETSKGT
60 70 80 90 100
SNDTKDPDNG EKNEEAAIDE NSNVEAAERK RKHISTDFSD DDLEKEEHND
110 120 130 140 150
QSLQPTVENR ASKDRDSSAT PSSRQELEEK LDRILKKPKV RRTRRDEDDL
160 170 180 190 200
EQYLDEKILR LKDEMNIAAQ LDIDTLNKRI ETGDTSLIAM QKVKLLPKVV
210 220 230 240 250
SVLSKANLAD TILDNNLLQS VRIWLEPLPD GSLPSFEIQK SLFAALNDLP
260 270 280 290 300
VKTEHLKESG LGRVVIFYTK SKRVEAQLAR LAEKLIAEWT RPIIGASDNY
310 320 330 340 350
RDKRIMQLEF DSEKLRKKSV MDSAKNRKKK SKSGEDPTSR GSSVQTLYEQ
360 370 380 390 400
AAARRNRAAA PAQTTTDYKY APVSNLSAVP TNARAVGVGS TLNNSEMYKR
410
LTSRLNKKHK
Length:410
Mass (Da):46,082
Last modified:November 1, 1996 - v1
Checksum:i7BC925FC8BA80E65
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40829 Genomic DNA. Translation: AAB68274.1.
AY558069 Genomic DNA. Translation: AAS56395.1.
BK006949 Genomic DNA. Translation: DAA11545.1.
PIRiS69023.
RefSeqiNP_015458.1. NM_001184230.1.

Genome annotation databases

EnsemblFungiiYPR133C; YPR133C; YPR133C.
GeneIDi856251.
KEGGisce:YPR133C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40829 Genomic DNA. Translation: AAB68274.1.
AY558069 Genomic DNA. Translation: AAS56395.1.
BK006949 Genomic DNA. Translation: DAA11545.1.
PIRiS69023.
RefSeqiNP_015458.1. NM_001184230.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NFQX-ray1.85A/B141-310[»]
3O8ZX-ray2.15A148-295[»]
3OAKX-ray2.15A/B148-292[»]
ProteinModelPortaliQ06505.
SMRiQ06505. Positions 148-295.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36299. 86 interactions.
DIPiDIP-3823N.
IntActiQ06505. 10 interactions.
MINTiMINT-529538.

PTM databases

iPTMnetiQ06505.

Proteomic databases

MaxQBiQ06505.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR133C; YPR133C; YPR133C.
GeneIDi856251.
KEGGisce:YPR133C.

Organism-specific databases

EuPathDBiFungiDB:YPR133C.
SGDiS000006337. SPN1.

Phylogenomic databases

GeneTreeiENSGT00720000108834.
HOGENOMiHOG000001004.
InParanoidiQ06505.
KOiK17498.
OMAiIGASDNY.
OrthoDBiEOG7N0CHQ.

Enzyme and pathway databases

BioCyciYEAST:G3O-34269-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ06505.
PROiQ06505.

Family and domain databases

Gene3Di1.20.930.10. 1 hit.
InterProiIPR017923. TFIIS_N.
[Graphical view]
PfamiPF08711. Med26. 1 hit.
[Graphical view]
PROSITEiPS51319. TFIIS_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "SPN1, a conserved gene identified by suppression of a postrecruitment-defective yeast TATA-binding protein mutant."
    Fischbeck J.A., Kraemer S.M., Stargell L.A.
    Genetics 162:1605-1616(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-192.
  5. "RNA polymerase II elongation factors of Saccharomyces cerevisiae: a targeted proteomics approach."
    Krogan N.J., Kim M., Ahn S.H., Zhong G., Kobor M.S., Cagney G., Emili A., Shilatifard A., Buratowski S., Greenblatt J.F.
    Mol. Cell. Biol. 22:6979-6992(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPT6, PHOSPHORYLATION AT SER-89.
  6. "Dual roles for Spt5 in pre-mRNA processing and transcription elongation revealed by identification of Spt5-associated proteins."
    Lindstrom D.L., Squazzo S.L., Muster N., Burckin T.A., Wachter K.C., Emigh C.A., McCleery J.A., Yates J.R. III, Hartzog G.A.
    Mol. Cell. Biol. 23:1368-1378(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ABD1; RBP1; SPT5 AND SPT6.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "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 SER-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-40 AND SER-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15; SER-23; SER-85; THR-86 AND SER-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiIWS1_YEAST
AccessioniPrimary (citable) accession number: Q06505
Secondary accession number(s): D6W4C9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 137 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 2830 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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