ATP-dependent RNA helicase DHX29 (DHX29)

The protein contains 1369 amino acids for an estimated molecular weight of 155236 Da.

 

ATP-binding RNA helicase involved in translation initiation. Part of the 43S pre-initiation complex that is required for efficient initiation on mRNAs of higher eukaryotes with structured 5'-UTRs by promoting efficient NTPase-dependent 48S complex formation. Specifically binds to the 40S ribosome near the mRNA entrance. Does not possess a processive helicase activity. (updated: Oct. 25, 2017)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  3. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

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: 45

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VariantDescription
dbSNP:rs35874395
dbSNP:rs17854904

The reference OMIM entry for this protein is 612720

Deah box polypeptide 29; dhx29

CLONING

Pisareva et al. (2008) purified Dhx29 from rabbit reticulocyte lysate and identified human DHX29 by database analysis. The deduced 1,369-amino acid human DHX29 protein contains a central DEAH box helicase domain and C-terminal helicase-associated HA2 and DUF1605 domains.

GENE FUNCTION

The 43S preinitiation complex containing 40S ribosomal subunits EIF3 (see 602039), EIF2 (see 603907), EIF1, EIF1A (EIF1AX; 300186), and initiator tRNA (see 180620) binds to and scans 5-prime UTRs of mRNAs to identify the initiation codon, where it stops to form the 48S initiation complex. Scanning of unstructured 5-prime UTRs does not require ATP or factors associated with ATP hydrolysis and RNA unwinding, whereas scanning of 5-prime UTRs with even weak secondary structure requires ATP and EIF4A (see 602641), EIF4G (see 600495), and EIF4B (603928). Pisareva et al. (2008) showed that rabbit Dhx29 was also required for efficient scanning of 5-prime UTRs with stable secondary structures. The extent of the requirement for Dhx29 correlated with the degree of stability in the secondary structure. Dhx29 bound 40S ribosomal subunits and hydrolyzed ATP, GTP, UTP, and CTP. NTPase activity of Dhx29 was strongly stimulated by 43S complexes, and Dhx29 stimulated 48S complex formation most strongly when it was present in substoichiometric amounts relative to 43S complexes. Rabbit Dhx29 did not show processive helicase activity.

MAPPING

Hartz (2009) mapped the DHX29 gene to chromosome 5q11.2 based on an alignment of the DHX29 gene (GenBank GENBANK AL079292) with the genomic sequence (build 36.1). ... More on the omim web site

Subscribe to this protein entry history

Feb. 5, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 612720 was added.