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PROSITE documentation PDOC00768 [for PROSITE entry PS51797]
Translationally controlled tumor protein (TCTP) domain signatures and profile


Description

The translationally controlled tumor proteins (TCTPs, such as p21, p23 and histamine releasing factor (HRF)) are a highly conserved and abundantly expressed family of eukaryotic proteins that are implicated in a variety of cellular functions, including microtubule stabilization, cell cycle, apoptosis, and cytokine release. TCTP is ubiquitously expressed in all eukaryotic organisms from protozoa such as Plasmodium sp. to plants and mammals [1,2,3,4].

The TCTP domain structure comprises four β-sheets, designated A-D, and three main helices, designated H1-H3, connected in a complex topology (see <PDB:1H7Y>). A central feature of the structure is the four-stranded sheet A, against one face of which packs the three-stranded sheet B and the small helix H1. Helix H3 packs against part of the opposite face of sheet A. Helix H2 packs against helix H3 (forming an α-helical hairpin). The final major structural feature is the two-stranded sheet C, which protrudes from the core globular structure formed by the rest of the domain [1].

As signature patterns for the TCTP domain, we selected two of the best conserved regions. We also developed a profile that covers the entire TCTP domain.

Last update:

May 2016 / Text revised; profile added.

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Technical section

PROSITE methods (with tools and information) covered by this documentation:

TCTP_3, PS51797; Translationally controlled tumor protein (TCTP) domain profile  (MATRIX)

TCTP_1, PS01002; Translationally controlled tumor protein (TCTP) domain signature 1  (PATTERN)

TCTP_2, PS01003; Translationally controlled tumor protein (TCTP) domain signature 2  (PATTERN)


References

1AuthorsThaw P. Baxter N.J. Hounslow A.M. Price C. Waltho J.P. Craven C.J.
TitleStructure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones.
SourceNat. Struct. Biol. 8:701-704(2001).
PubMed ID11473261
DOI10.1038/90415

2AuthorsChoi K.-W. Hsu Y.-C.
TitleTo cease or to proliferate: new insights into TCTP function from a Drosophila study.
SourceCell Adh. Migr. 1:129-130(2007).
PubMed ID19262129

3AuthorsSusini L. Besse S. Duflaut D. Lespagnol A. Beekman C. Fiucci G. Atkinson A.R. Busso D. Poussin P. Marine J.-C. Martinou J.-C. Cavarelli J. Moras D. Amson R. Telerman A.
TitleTCTP protects from apoptotic cell death by antagonizing bax function.
SourceCell Death Differ. 15:1211-1220(2008).
PubMed ID18274553
DOI10.1038/cdd.2008.18

4AuthorsEichhorn T. Winter D. Buchele B. Dirdjaja N. Frank M. Lehmann W.D. Mertens R. Krauth-Siegel R.L. Simmet T. Granzin J. Efferth T.
TitleMolecular interaction of artemisinin with translationally controlled tumor protein (TCTP) of Plasmodium falciparum.
SourceBiochem. Pharmacol. 85:38-45(2013).
PubMed ID23085438
DOI10.1016/j.bcp.2012.10.006



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