DNA transposase THAP9 (THAP9)

The protein contains 903 amino acids for an estimated molecular weight of 103411 Da.

 

Active transposase that specifically recognizes the bipartite 5'-TXXGGGX(A/T)-3' consensus motif and mediates transposition. (updated: Sept. 12, 2018)

Protein identification was indicated in the following studies:

  1. 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.

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VariantDescription
dbSNP:rs1031639
dbSNP:rs897945
dbSNP:rs6535411
dbSNP:rs35532215

No binding partner found

The reference OMIM entry for this protein is 612537

Thap domain-containing protein 9; thap9

CLONING

By searching databases, Roussigne et al. (2003) identified several proteins containing an N-terminal THAP domain, including THAP9. The THAP domain of the deduced 903-amino acid THAP9 protein includes a C2CH signature, an AVPTIF box, and several other conserved amino acids. The THAP domain is followed by a stretch that shares similarity with the Drosophila P element transposase.

MAPPING

Hartz (2009) mapped the THAP9 gene to chromosome 4q21.22 based on an alignment of the THAP9 sequence (GenBank GENBANK AK026973) with the genomic sequence (build 36.1).

GENE FUNCTION

Majumdar et al. (2013) showed that human THAP9 can mobilize Drosophila P elements in both Drosophila and human cells. Chimeric proteins formed between the Drosophila P element transposase N-terminal THAP DNA-binding domain; the C-terminal regions of human THAP9 can also mobilize Drosophila P elements. Majumdar et al. (2013) concluded that human THAP9 is an active DNA transposase that, although 'domesticated,' still retains the catalytic activity to mobilize P transposable elements across species. ... More on the omim web site

Subscribe to this protein entry history

June 30, 2020: Protein entry updated
Automatic update: OMIM entry 612537 was added.

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