Summary: Translationally controlled tumour protein
This is the Wikipedia entry entitled "Translationally controlled tumour protein". More...
The Wikipedia text that you see displayed here is a download from Wikipedia. This means that the information we display is a copy of the information from the Wikipedia database. The button next to the article title ("Edit Wikipedia article") takes you to the edit page for the article directly within Wikipedia. You should be aware you are not editing our local copy of this information. Any changes that you make to the Wikipedia article will not be displayed here until we next download the article from Wikipedia. We currently download new content on a nightly basis.
Does Pfam agree with the content of the Wikipedia entry ?
Pfam has chosen to link families to Wikipedia articles. In some case we have created or edited these articles but in many other cases we have not made any direct contribution to the content of the article. The Wikipedia community does monitor edits to try to ensure that (a) the quality of article annotation increases, and (b) vandalism is very quickly dealt with. However, we would like to emphasise that Pfam does not curate the Wikipedia entries and we cannot guarantee the accuracy of the information on the Wikipedia page.
Editing Wikipedia articles
Before you edit for the first time
Wikipedia is a free, online encyclopedia. Although anyone can edit or contribute to an article, Wikipedia has some strong editing guidelines and policies, which promote the Wikipedia standard of style and etiquette. Your edits and contributions are more likely to be accepted (and remain) if they are in accordance with this policy.
You should take a few minutes to view the following pages:
How your contribution will be recorded
Anyone can edit a Wikipedia entry. You can do this either as a new user or you can register with Wikipedia and log on. When you click on the "Edit Wikipedia article" button, your browser will direct you to the edit page for this entry in Wikipedia. If you are a registered user and currently logged in, your changes will be recorded under your Wikipedia user name. However, if you are not a registered user or are not logged on, your changes will be logged under your computer's IP address. This has two main implications. Firstly, as a registered Wikipedia user your edits are more likely seen as valuable contribution (although all edits are open to community scrutiny regardless). Secondly, if you edit under an IP address you may be sharing this IP address with other users. If your IP address has previously been blocked (due to being flagged as a source of 'vandalism') your edits will also be blocked. You can find more information on this and creating a user account at Wikipedia.
If you have problems editing a particular page, contact us at email@example.com and we will try to help.
The community annotation is a new facility of the Pfam web site. If you have problems editing or experience problems with these pages please contact us.
Translationally controlled tumour protein Edit Wikipedia article
|This article is an orphan, as no other articles link to it. Please introduce links to this page from ; try the Find link tool for suggestions. (February 2009)|
translationally controlled tumor-associated protein p23fyp from schizosaccharomyces pombe
|Translationally Controlled Tumour Protein|
|Symbol||FLJ27337,tpt1,HRF, p02, p23, p21|
In molecular biology, the protein TCTP, is short for translationally controlled tumour protein (TCTP).The translationally controlled tumour protein, commonly known as TCTP, is a highly conserved protein among many eukaryotic organisms. TCTP is involved in a variety of cellular activities, including microtubule stabilization, calcium-binding activities, and apoptosis. The Mammalian translationally controlled tumour protein (TCTP) (or P23) is a protein which has been found to be preferentially synthesised in cells during the early growth phase of some types of tumour, but which is also expressed in normal cells. It was first identified as a histamine-releasing factor, acting in IgE +-dependent allergic reactions. In addition, TCTP has been shown to bind to tubulin in the cytoskeleton, has a high affinity for calcium, is the binding target for the antimalarial compound artemisinin, and is induced in vitamin D-dependent apoptosis. TCTP production is thought to be controlled at the translational as well as the transcriptional level.
TCTP is a hydrophilic protein of 18 to 20 kD. TCTPs do not share significant sequence similarity with any other class of proteins. Recently, the structure of TCTP was determined and exhibited significant structural similarity to the human protein Mss4, which is a guanine nucleotide-free chaperone of the Rab protein. Translationally controlled tumor protein (TCTP) is a highly conserved protein found in eukaryotes, across animal and plant kingdoms and even in yeast. Close homologues have been found in plants, earthworm, Caenorhabditis elegans (F52H2.11), Hydra, Saccharomyces cerevisiae (YKL056c)  and Schizosaccharomyces pombe (SpAC1F12.02c). Mammalian TCTP is ubiquitously expressed in various tissues and cell types.
Translationally-controlled tumor-associated protein (TCTP) has many roles in cellular processes, most notably in the following:
- embryo development,
- cell cycle,
- Cell proliferation,
- stress response,
- gene regulation,
- heat shock
In essence, TCTP functions as molecule that prevents cell death. It reduces cellular stress working as a heat shock protein and a molecular chaperone. It prevents cell death by binding to calcium, an ion that causes cell death. Furthermore, the N-terminal domain of TCTP inhibits apoptosis by binding to apoptotic factors and by inhibiting p53 tumour suppressor-dependent apoptosis by downregulating it.
TCTP interacts with F-actin and mitotic spindle  and regulates cell shape by interacting with the cytoskeleton. Since most cellular processes, such as the cell cycle and cancer, involve changes in the cytoskeleton; it becomes apparent why TCTP is important. Moreover, if the gene encoding TCTP is knocked-out in mice, it becomes embryonic lethal, and they die in utero (in the womb).
- Ulrich-Axel Bommer, Bernd-Joachim Thiele (2004). "The translationally controlled tumour protein (TCTP)". IJBCB 36 (3): 379–385. doi:10.1016/S1357-2725(03)00213-9. PMID 14687915.
- BÃ¶hm H, Benndorf R, Gaestel M, Gross B, NÃ¼rnberg P, Kraft R, Otto A, Bielka H (August 1989). "The growth-related protein P23 of the Ehrlich ascites tumor: translational control, cloning and primary structure". Biochem. Int. 19 (2): 277–86. PMID 2479380.
- Chitpatima ST, Makrides S, Bandyopadhyay R, Brawerman G (March 1988). "Nucleotide sequence of a major messenger RNA for a 21 kilodalton polypeptide that is under translational control in mouse tumor cells". Nucleic Acids Res. 16 (5): 2350. doi:10.1093/nar/16.5.2350. PMC 338237. PMID 3357792.
- Thiele H, Berger M, Skalweit A, Thiele BJ (September 2000). "Expression of the gene and processed pseudogenes encoding the human and rabbit translationally controlled tumour protein (TCTP)". Eur. J. Biochem. 267 (17): 5473–81. doi:10.1046/j.1432-1327.2000.01609.x. PMID 10951206.
- Thaw P, Baxter NJ, Hounslow AM, Price C, Waltho JP, Craven CJ (August 2001). "Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones". Nat. Struct. Biol. 8 (8): 701–4. doi:10.1038/90415. PMID 11473261.
- Pay A, Heberle-Bors E, Hirt H (June 1992). "An alfalfa cDNA encodes a protein with homology to translationally controlled human tumor protein". Plant Mol. Biol. 19 (3): 501–3. doi:10.1007/bf00023399. PMID 1623194.
- StÃ¼rzenbaum SR, Kille P, Morgan AJ (July 1998). "Identification of heavy metal induced changes in the expression patterns of the translationally controlled tumour protein (TCTP) in the earthworm Lumbricus rubellus1". Biochim. Biophys. Acta 1398 (3): 294–304. doi:10.1016/s0167-4781(98)00077-3. PMID 9655922.
- Rasmussen SW (April 1994). "Sequence of a 28.6 kb region of yeast chromosome XI includes the FBA1 and TOA2 genes, an open reading frame (ORF) similar to a translationally controlled tumour protein, one ORF containing motifs also found in plant storage proteins and 13 ORFs with weak or no homology to known proteins". Yeast. 10 Suppl A: S63–8. doi:10.1002/yea.320100008. PMID 8091862.
- Nagano-Ito M, Ichikawa S (2012). "Biological effects of Mammalian translationally controlled tumor protein (TCTP) on cell death, proliferation, and tumorigenesis.". Biochem Res Int 2012: 204960. doi:10.1155/2012/204960. PMC 3364544. PMID 22675633.
- PMID 10085260
- Bazile F, Pascal A, Arnal I, Le Clainche C, Chesnel F, Kubiak JZ (2009). "Complex relationship between TCTP, microtubules and actin microfilaments regulates cell shape in normal and cancer cells.". Carcinogenesis 30 (4): 555–65. doi:10.1093/carcin/bgp022. PMC 2831045. PMID 19168579.
Translationally controlled tumour protein Provide feedback
No Pfam abstract.
Internal database links
|SCOOP:||URO-D Glyco_hydro_14 Endotoxin_N DUF2766|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR018105
Mammalian translationally controlled tumour protein (TCTP) (or P23) is a protein which has been found to be preferentially synthesised in cells during the early growth phase of some types of tumour [PUBMED:2479380, PUBMED:3357792], but which is also expressed in normal cells. The physiological function of TCTP is still not known. It was first identified as a histamine-releasing factor, acting in IgE +-dependent allergic reactions. In addition, TCTP has been shown to bind to tubulin in the cytoskeleton, has a high affinity for calcium, is the binding target for the antimalarial compound artemisinin, and is induced in vitamin D-dependent apoptosis. TCTP production is thought to be controlled at the translational as well as the transcriptional level [PUBMED:10951206].
TCTP is a hydrophilic protein of 18 to 20 kD. TCTPs do not share significant sequence similarity with any other class of proteins. Recently, the structure of TCTP was determined and exhibited significant structural similarity to the human protein Mss4, which is a guanine nucleotide-free chaperone of the Rab protein [PUBMED:11473261]. Close homologues have been found in plants [PUBMED:1623194], earthworm [PUBMED:9655922], Caenorhabditis elegans (F52H2.11), Hydra, Saccharomyces cerevisiae (YKL056c) [PUBMED:8091862] and Schizosaccharomyces pombe (SpAC1F12.02c).
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
- the number of residues in the sequence
- the Pfam graphic itself.
Loading domain graphics...
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
- Pfam viewer
- an HTML-based viewer that uses DAS to retrieve alignment fragments on request
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
Format an alignment
If you find these logos useful in your own work, please consider citing the following article:
Note: You can also download the data file for the tree.
Curation and family details
|Seed source:||Pfam-B_1548 (release 2.1)|
|Number in seed:||168|
|Number in full:||1065|
|Average length of the domain:||150.70 aa|
|Average identity of full alignment:||39 %|
|Average coverage of the sequence by the domain:||85.27 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|Download:||download the raw HMM for this family|
Weight segments by...
Change the size of the sunburst
selected sequences to HMM
a FASTA-format file
- 0 sequences
- 0 species
How the sunburst is generated
Colouring and labels
Anomalies in the taxonomy tree
Missing taxonomic levels
Unmapped species names
Too many species/sequences
The tree shows the occurrence of this domain across different species. More...
You can use the tree controls to manipulate how the interactive tree is displayed:
- show/hide the summary boxes
- highlight species that are represented in the seed alignment
- expand/collapse the tree or expand it to a given depth
- select a sub-tree or a set of species within the tree and view them graphically or as an alignment
- save a plain text representation of the tree
There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the TCTP domain has been found. There are 15 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
Loading structure mapping...