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22  structures 312  species 0  interactions 874  sequences 15  architectures

Family: TACC_C (PF05010)

Summary: Transforming acidic coiled-coil-containing protein (TACC), C-terminal

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Transforming acidic coiled-coil-containing protein (TACC), C-terminal Provide feedback

This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organising centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1) [1]. TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis [2]. Maskin is also found to bind CPEB and elF-4E [3]. Interestingly, the functional homologue (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organisation of bipolar spindles [4].

Literature references

  1. Gergely F, Karlsson C, Still I, Cowell J, Kilmartin J, Raff JW; , Proc Natl Acad Sci U S A 2000;97:14352-14357.: The TACC domain identifies a family of centrosomal proteins that can interact with microtubules. PUBMED:11121038 EPMC:11121038

  2. Mortuza GB, Cavazza T, Garcia-Mayoral MF, Hermida D, Peset I, Pedrero JG, Merino N, Blanco FJ, Lyngso J, Bruix M, Pedersen JS, Vernos I, Montoya G;, Nat Commun. 2014;5:5072.: XTACC3-XMAP215 association reveals an asymmetric interaction promoting microtubule elongation. PUBMED:25262927 EPMC:25262927

  3. Stebbins-Boaz B, Cao Q, de Moor CH, Mendez R, Richter JD;, Mol Cell. 1999;4:1017-1027. : Maskin is a CPEB-associated factor that transiently interacts with elF-4E. PUBMED:10635326 EPMC:10635326

  4. Sato M, Vardy L, Angel Garcia M, Koonrugsa N, Toda T; , Mol Biol Cell. 2004;15:1609-1622.: Interdependency of fission yeast Alp14/TOG and coiled coil protein Alp7 in microtubule localization and bipolar spindle formation. PUBMED:14742702 EPMC:14742702


Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR007707

This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organising centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1) [PUBMED:11121038]. TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis [PUBMED:25262927]. Maskin is also found to bind CPEB and elF-4E [PUBMED:10635326]. Interestingly, the functional homologue (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organisation of bipolar spindles [PUBMED:14742702].

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan TACC (CL0679), which has the following description:

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].

The clan contains the following 2 members:

Fungal_TACC TACC_C

Alignments

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(27)
Full
(874)
Representative proteomes UniProt
(1462)
NCBI
(3888)
Meta
(0)
RP15
(178)
RP35
(329)
RP55
(553)
RP75
(643)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

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  Seed
(27)
Full
(874)
Representative proteomes UniProt
(1462)
NCBI
(3888)
Meta
(0)
RP15
(178)
RP35
(329)
RP55
(553)
RP75
(643)
Alignment:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(27)
Full
(874)
Representative proteomes UniProt
(1462)
NCBI
(3888)
Meta
(0)
RP15
(178)
RP35
(329)
RP55
(553)
RP75
(643)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download    
Gzipped Download   Download   Download   Download   Download   Download   Download   Download    

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_4807 (release 7.6)
Previous IDs: TACC;
Type: Coiled-coil
Sequence Ontology: SO:0001080
Author: Moxon SJ , Sangrador A , El-Gebali S
Number in seed: 27
Number in full: 874
Average length of the domain: 188.30 aa
Average identity of full alignment: 41 %
Average coverage of the sequence by the domain: 20.83 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 29.9 29.9
Trusted cut-off 29.9 30.1
Noise cut-off 29.7 29.1
Model length: 201
Family (HMM) version: 14
Download: download the raw HMM for this family

Species distribution

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Structures

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 TACC_C domain has been found. There are 22 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 sequence.

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