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Protein

RNA-induced transcriptional silencing complex protein tas3

Gene

tas3

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

Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation and accurate chromosome segregation. A member of the RNA-induced transcriptional silencing (RITS) complex which is involved in the biosynthesis of dsRNA from primer siRNAs provided by the RNA-directed RNA polymerase (RDRC) complex.2 Publications

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cellular protein localization Source: PomBase
  • chromatin silencing at silent mating-type cassette Source: PomBase
  • chromatin silencing by small RNA Source: PomBase
  • chromosome segregation Source: UniProtKB-KW
  • regulation of chromatin silencing at centromere Source: PomBase
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Chromosome partition, RNA-mediated gene silencing

Names & Taxonomyi

Protein namesi
Recommended name:
RNA-induced transcriptional silencing complex protein tas3
Short name:
RITS protein tas3
Gene namesi
Name:tas3
ORF Names:SPBC83.03c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC83.03c.
PomBaseiSPBC83.03c. tas3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-KW
  • mating-type region heterochromatin Source: PomBase
  • mitotic spindle pole body Source: PomBase
  • nuclear pericentric heterochromatin Source: PomBase
  • nuclear subtelomeric heterochromatin Source: PomBase
  • nucleus Source: PomBase
  • RITS complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 549549RNA-induced transcriptional silencing complex protein tas3PRO_0000256153Add
BLAST

Proteomic databases

MaxQBiO94687.

Interactioni

Subunit structurei

Ago1, chp1 and tas3 interact to form the core of the RNA-induced transcriptional silencing (RITS) complex. The RITS complex interacts with the RDRC complex via interaction between ago1 and hrr1. Clr4 has a role in mediating this interaction.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
chp1Q101033EBI-423002,EBI-421832

Protein-protein interaction databases

BioGridi277258. 311 interactions.
DIPiDIP-29302N.
IntActiO94687. 2 interactions.
MINTiMINT-4686205.

Structurei

Secondary structure

1
549
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 113Combined sources
Helixi12 – 176Combined sources
Helixi29 – 4921Combined sources
Helixi50 – 534Combined sources
Helixi58 – 7922Combined sources
Helixi435 – 44410Combined sources
Helixi447 – 4504Combined sources
Helixi453 – 46715Combined sources
Helixi473 – 4819Combined sources
Helixi495 – 50511Combined sources
Helixi510 – 52617Combined sources
Helixi530 – 54314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3D1BX-ray1.70A/B/C426-545[»]
3D1DX-ray2.60A/B/C/D/E/F426-545[»]
3TIXX-ray2.90A/C9-83[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO94687.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi167 – 22559Ser-richAdd
BLAST

Phylogenomic databases

OrthoDBiEOG7BW0WB.

Family and domain databases

InterProiIPR019486. Argonaute_hook_dom.
[Graphical view]
PfamiPF10427. Ago_hook. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O94687-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKGIKKYLP SLPFLACISD FPENHGTSRR SATVSLERVH ELFTEHWLSN
60 70 80 90 100
LKNRREKRQE LAEEAVYCRS EMLSQRKLLA AVDFPQQLKN SPAKAKATHT
110 120 130 140 150
SSGVTKEVRA SKKYTSSNVE FPLVTDGKEK PVKSKQLRKN SVTEFEKPIE
160 170 180 190 200
TKKSKHRKSR NKFLDKSSGS MEIESWDNST SDSIIESSSR LHESISLREN
210 220 230 240 250
DIRSSDSKSV GWDDNSTGFR ESSKSLDHTD TSMFMELDSN SDPQFRPKYQ
260 270 280 290 300
AKSSWFAPDD PEASWGNLDD GWGETNGSWS STDDTKHYKN EWAESINLDN
310 320 330 340 350
FNRPSQQEDY DKPKNTQVSR SSNHHRRYDS YHPDSRSDSY RSKREHYDNR
360 370 380 390 400
DTGPRSKHLE KSSYVYNQNF EDRTHLSDHG AHFHLGNAND FNMQGSSRKR
410 420 430 440 450
KASDRQRESR ENELPTKKLN ASDSHNPLAS LTTDKNDLYI NWLKSLSFFQ
460 470 480 490 500
TNSSCAEALV KVIPHYHNKL IDFSQVLQLV FSASEKFPIQ ENQPLPEQLM
510 520 530 540
FLSNLEKQTP FAKAVGSSIY KLVTGKNLSL DFASQILKEA SILEHKNEK
Length:549
Mass (Da):63,056
Last modified:May 1, 1999 - v1
Checksum:i4569CF59851A22A0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB36865.1.
PIRiT40692.
RefSeqiNP_595635.1. NM_001021529.2.

Genome annotation databases

EnsemblFungiiSPBC83.03c.1; SPBC83.03c.1:pep; SPBC83.03c.
GeneIDi2540735.
KEGGispo:SPBC83.03c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB36865.1.
PIRiT40692.
RefSeqiNP_595635.1. NM_001021529.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3D1BX-ray1.70A/B/C426-545[»]
3D1DX-ray2.60A/B/C/D/E/F426-545[»]
3TIXX-ray2.90A/C9-83[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277258. 311 interactions.
DIPiDIP-29302N.
IntActiO94687. 2 interactions.
MINTiMINT-4686205.

Proteomic databases

MaxQBiO94687.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC83.03c.1; SPBC83.03c.1:pep; SPBC83.03c.
GeneIDi2540735.
KEGGispo:SPBC83.03c.

Organism-specific databases

EuPathDBiFungiDB:SPBC83.03c.
PomBaseiSPBC83.03c. tas3.

Phylogenomic databases

OrthoDBiEOG7BW0WB.

Miscellaneous databases

EvolutionaryTraceiO94687.
PROiO94687.

Family and domain databases

InterProiIPR019486. Argonaute_hook_dom.
[Graphical view]
PfamiPF10427. Ago_hook. 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. "Two RNAi complexes, RITS and RDRC, physically interact and localize to noncoding centromeric RNAs."
    Motamedi M.R., Verdel A., Colmenares S.U., Gerber S.A., Gygi S.P., Moazed D.
    Cell 119:789-802(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COMPOSITION OF THE RDRC AND RITS COMPLEXES, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  3. "RNAi-mediated targeting of heterochromatin by the RITS complex."
    Verdel A., Jia S., Gerber S., Sugiyama T., Gygi S.P., Grewal S.I.S., Moazed D.
    Science 303:672-676(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COMPOSITION OF THE RITS COMPLEX, INTERACTION WITH CHP1.
  4. "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 nameiTAS3_SCHPO
AccessioniPrimary (citable) accession number: O94687
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: May 1, 1999
Last modified: June 8, 2016
This is version 87 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: 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.