Transforming acidic coiled-coil

TACC proteins are present in different organisms, ranging from yeasts to mammals. For example, TACC proteins can be found in: Caenorhabditis elegans (TAC-1), Drosophila melanogaster (D-TACC), Xenopus laevis (Maskin), and in the fission yeast Schizosaccharomyces pombe (Alp7 also known as Mia1p); by contrast, mammals have three such proteins (TACC1, TACC2 [also known as AZU-1 and ECTACC] and TACC3 [also known as AINT and ERIC1]). Alternative splicing further increases the complexity of the TACC protein family in mammals and flies . The first member of the TACC family to be discovered was identified in a search of genomic regions that are amplified in breast cancer. It was named transforming acidic coiled-coil 1 (TACC1) because of its highly acidic nature, the presence of a predicted coiled-coil domain at its C terminus (now known as the TACC domain), and its ability to promote cellular transformation. one of the extensively characterised TACC proteins, Maskin acts as a factor involved in the regulation of mRNA translation during maturation of Xenopus oocytes. Other TACC family members have also been implicated in various events related to gene regulation, including the regulation of translation, RNA maturation and gene expression. Furthermore, TACC proteins have a role in regulating microtubule assembly such as D-TACC which acts as a Drosophila microtubule-associated and centrosomal protein required for centrosome activity and microtubule assembly during mitosis [1].

This clan contains 2 families and the total number of domains in the clan is 2893. The clan was built by S El-Gebali.

Literature references

1. Peset I, Vernos I;, Trends Cell Biol. 2008;18:379-388.: The TACC proteins: TACC-ling microtubule dynamics and centrosome function. PUBMED:18656360 EPMC:18656360

Members

This clan contains the following 2 member families:

Below is a listing of the unique domain organisations or architectures from this clan. More...

The table below shows the number of occurrences of each domain throughout the sequence database. More...

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This diagram shows the relationships between members of this clan. More...

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between the Pfam families in this clan, the corresponding UniProt entries, and the region of the three-dimensional structures that are available for that sequence.