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Protein

Transcriptional repressor tup11

Gene

tup11

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional repressor.

GO - Molecular functioni

  • histone binding Source: PomBase

GO - Biological processi

  • chromatin silencing Source: PomBase
  • negative regulation of transcription by glucose Source: PomBase
  • negative regulation of transcription from RNA polymerase II promoter Source: PomBase
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional repressor tup11
Gene namesi
Name:tup11
ORF Names:SPAC18B11.10
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC18B11.10.
PomBaseiSPAC18B11.10. tup11.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • nuclear chromatin Source: PomBase
  • nuclear transcriptional repressor complex Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi362 – 3621Y → C: No interaction with fep1. 1 Publication
Mutagenesisi542 – 5421L → S: No interaction with fep1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 614614Transcriptional repressor tup11PRO_0000051310Add
BLAST

Proteomic databases

MaxQBiQ09715.

Interactioni

Subunit structurei

Interacts with fep1. Binds to histones H3 and H4.1 Publication

GO - Molecular functioni

  • histone binding Source: PomBase

Protein-protein interaction databases

BioGridi278766. 30 interactions.
MINTiMINT-730832.

Structurei

3D structure databases

ProteinModelPortaliQ09715.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati311 – 34030WD 1Add
BLAST
Repeati358 – 38831WD 2Add
BLAST
Repeati400 – 43031WD 3Add
BLAST
Repeati441 – 47131WD 4Add
BLAST
Repeati482 – 51231WD 5Add
BLAST
Repeati536 – 56631WD 6Add
BLAST
Repeati578 – 60831WD 7Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat TUP1 family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

HOGENOMiHOG000200558.
InParanoidiQ09715.
KOiK06666.
OMAiRARIWSI.
OrthoDBiEOG7TN01P.
PhylomeDBiQ09715.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR013890. Tscrpt_rep_Tup1_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08581. Tup_N. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
ProDomiPD010558. Transcrip_repressor_Tup1_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q09715-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASVEDATKV QEMLDALKAE YNALAHHSFA SKARGNDYES SMIQSQIQEI
60 70 80 90 100
EAFRKTVDDM YEKQKSIRET YEKDINKLKR ELEELGVEAN TASYRNRGER
110 120 130 140 150
SELAASNNQV THIDQEHPSQ TKSTSQPPSN HLPAFQQIPP IHQSAYPQNN
160 170 180 190 200
VAEVLMPPIP PSVEASSGQN FNQGIASQNP AISTSNLPST TPLYIPPVNY
210 220 230 240 250
GANQVSQQPN PQLPGVSNYY NPSATSKPAV NVQPPRIPTK ATPSAEPSMT
260 270 280 290 300
ASANAGSISQ AGPDGEYQGR EQIAPVSDTE AARKTTSQSW YVTYNPACKR
310 320 330 340 350
VFNINLVHTL EHPSVVCCVK FSNNGKYLAT GCNQAANVFD VQTGKKLFTL
360 370 380 390 400
HEESPDPSRD LYVRTIAFSP DGKYLVTGTE DRQIKLWDLS TQKVRYVFSG
410 420 430 440 450
HEQDIYSLDF SHNGRFIVSG SGDRTARLWD VETGQCILKL EIENGVTAIA
460 470 480 490 500
ISPNDQFIAV GSLDQIIRVW SVSGTLVERL EGHKESVYSI AFSPDSSILL
510 520 530 540 550
SGSLDKTIKV WELQATRSVG LSAIKPEGIC KATYTGHTDF VLSVAVSPDS
560 570 580 590 600
RWGLSGSKDR SMQFWDLQTG QSYLTCQGHK NSVISVCFSP DGRQFASGSG
610
DLRARIWSID PASP
Length:614
Mass (Da):67,331
Last modified:November 1, 1995 - v1
Checksum:iB02289556DE2C1B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA90594.1.
AB027768 Genomic DNA. Translation: BAA87072.1.
PIRiS58306.
RefSeqiNP_592873.1. NM_001018273.2.

Genome annotation databases

EnsemblFungiiSPAC18B11.10.1; SPAC18B11.10.1:pep; SPAC18B11.10.
GeneIDi2542299.
KEGGispo:SPAC18B11.10.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA90594.1.
AB027768 Genomic DNA. Translation: BAA87072.1.
PIRiS58306.
RefSeqiNP_592873.1. NM_001018273.2.

3D structure databases

ProteinModelPortaliQ09715.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278766. 30 interactions.
MINTiMINT-730832.

Proteomic databases

MaxQBiQ09715.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC18B11.10.1; SPAC18B11.10.1:pep; SPAC18B11.10.
GeneIDi2542299.
KEGGispo:SPAC18B11.10.

Organism-specific databases

EuPathDBiFungiDB:SPAC18B11.10.
PomBaseiSPAC18B11.10. tup11.

Phylogenomic databases

HOGENOMiHOG000200558.
InParanoidiQ09715.
KOiK06666.
OMAiRARIWSI.
OrthoDBiEOG7TN01P.
PhylomeDBiQ09715.

Miscellaneous databases

NextBioi20803361.
PROiQ09715.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR013890. Tscrpt_rep_Tup1_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08581. Tup_N. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
ProDomiPD010558. Transcrip_repressor_Tup1_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library."
    Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y.
    Genes Cells 5:169-190(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 71-101, SUBCELLULAR LOCATION.
    Strain: ATCC 38364 / 968.
  3. "Conservation of histone binding and transcriptional repressor functions in a Schizosaccharomyces pombe Tup1p homolog."
    Mukai Y., Matsuo E., Roth S.Y., Harashima S.
    Mol. Cell. Biol. 19:8461-8468(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. "The Schizosaccharomyces pombe corepressor Tup11 interacts with the iron-responsive transcription factor Fep1."
    Znaidi S., Pelletier B., Mukai Y., Labbe S.
    J. Biol. Chem. 279:9462-9474(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FEP1, MUTAGENESIS OF TYR-362 AND LEU-542.
  5. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTUP11_SCHPO
AccessioniPrimary (citable) accession number: Q09715
Secondary accession number(s): Q9USG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.