Translationally-controlled tumor protein (TPT1)

The protein contains 172 amino acids for an estimated molecular weight of 19595 Da.

 

Involved in calcium binding and microtubule stabilization. (updated: Sept. 12, 2018)

Protein identification was indicated in the following studies:

  1. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  2. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  3. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 0%
Model score: 0
No model available.

(right-click above to access to more options from the contextual menu)

VariantDescription
dbSNP:rs3087989

The reference OMIM entry for this protein is 600763

Tumor protein, translationally-controlled 1; tpt1
Translationally controlled tumor protein; tctp
Histamine-releasing factor, immunoglobulin e-dependent; hrf

CLONING

MacDonald et al. (1995) stated that several in vivo systems are used to study human allergic disease. A favored model is the late response in humans that occurs hours after the immediate reaction to allergen challenge. The pathophysiologic events, such as decreased airway function, are characterized by infiltration of inflammatory cells and by the presence of mediators such as histamine, which are findings similar to those observed in people with chronic allergic diseases such as asthma. The histamine released in this late-phase reaction (LPR) results from activation of basophils that, along with eosinophils and lymphocytes, infiltrate tissues during this response. Because the allergen that initiated the response is no longer present, 2 questions required study: the nature of the agent that triggers the release of inflammatory mediators from the basophils in the LPR, and the basis for the observation that only about half of allergic individuals experience an LPR. MacDonald et al. (1995) identified and purified an immunoglobulin E (IgE; 147180)-dependent histamine-releasing factor, which they symbolized HRF, produced by lymphocytes of atopic children and present in biologic fluids of allergic patients. Amino-terminal sequencing revealed extensive homology to the mouse protein p21 and identity to its human homolog, p23, described by Bohm et al. (1989) and Bohm et al. (1991).

GENE FUNCTION

MacDonald et al. (1995) showed that both human and mouse recombinant HRF proteins caused histamine release from human basophils of a subpopulation of donors, and this release was dependent on IgE. Polyclonal antibodies raised in the rabbit against recombinant mouse Hrf recognized and removed the biologic activity of both recombinant and native HRF. HRF identifies heterogeneity of IgE, which may be a genetically determined polymorphism, may be due to differential glycosylation of the IgE molecule, or may be based on interactions with the alternatively spliced forms of human IgE reported to be present in human atopic serum (Zhang et al., 1992; see 147180). Amzallag et al. (2004) found that secretion of TPT1 proceeded by a nonclassical pathway independent of the endoplasmic reticulum and Golgi apparatus. Secreted TPT1 appeared to originate from preexisting pools. Amzallag et al. (2004) determined that TSAP6 (STEAP3; 609671) interacted with TPT1 in several protein interaction assays, and the 2 proteins codistributed to small vesicles called exosomes at the plasma membrane and around the nucleus in several human cell lines. Overexpression of TSAP6 increased the level of TPT1 in exosome preparations and consistently enhanced TPT1 secretion. Hsu et al. (2007) demonstrated that a conserved protein, TCTP, is an essential component of the tuberous sclerosis (see TSC1, 605284)-RHEB (601293) pathway. Reducing Drosophila Tctp levels reduced cell size, cell number, and organ size, which mimics Drosophila Rheb mutant phenotypes. Drosophila Tctp is genetically epistatic to Tsc1 and Rheb, but acts upstream of S6K (see 608938), a downstream target of Rheb. Drosophila Tctp directly associated with Rheb and displayed guanine nucleotide exchange activity with it in vivo and in vitro. Human TCTP showed similar biochemical properties compared to Drosophila Tctp and could rescue Drosophila Tctp mutant phenotypes, suggesting that the function of TCTP in the TSC pathway is evolutionarily conserved. Hsu et al. (2007) concluded that their studies ident ... More on the omim web site

Subscribe to this protein entry history

June 30, 2020: Protein entry updated
Automatic update: OMIM entry 600763 was added.

Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).