60S ribosomal protein L29 (RPL29)
The protein contains 159 amino acids for an estimated molecular weight of 17752 Da.
Component of the large ribosomal subunit. (updated: Oct. 10, 2018)
Protein identification was indicated in the following studies:
- 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.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- 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.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
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.
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The reference OMIM entry for this protein is 601832
Ribosomal protein l29; rpl29
Hp/hs-interacting protein; hip
Heparin/heparan sulfate-binding protein
CLONING
Liu et al. (1996) used RT-PCR to identify transcripts encoding cell surface heparin/heparan sulfate- (HP/HS-) binding peptides. One clone isolated in this manner had a predicted peptide sequence with features of an HP/HS-binding motif; the authors termed this transcript HIP, for 'HP/HS interacting protein.' Liu et al. (1996) cloned the corresponding cDNA from a HeLa cell cDNA library and found that it encodes a 159-amino acid polypeptide 80% similar to the rodent ribosomal protein L29. Transfection of HIP cDNA demonstrated cell surface expression, and the sequence encodes neither a membrane-spanning region nor a glycosylation site. Northern blot analysis revealed that HIP is expressed as a 1.3-kb message in a variety of human cell lines and tissues. Mammalian ribosome proteins are members of multigene families that are composed predominantly of multiple processed pseudogenes and 1 functional-containing gene, although some, such as human ribosomal protein L37a, are present as single-copy genes. During a large-scale partial sequencing of human heart cDNA clones, Law et al. (1996) found a novel clone that was very similar to the rat ribosomal protein L29 in both DNA and amino acid sequences. The cDNA encodes a protein that shows 80.4% homology to protein L29 from the large ribosomal subunit of rat. The putative protein has a large excess of basic residues over acidic residues, with a unique lysine-rich tandem repeat structure that suggested a binding function. Liu et al. (1996) showed that RPL29 had the same nucleotide sequence as does cell surface heparin/heparan sulfate-binding protein, also designated HB/HS interacting protein.GENE FUNCTION
Rohde et al. (1996) demonstrated direct binding between heparin and HIP. They showed that HIP is expressed on the surfaces of intact RL95 uterine epithelial cells and that RL95 cell suspensions form aggregates when incubated with antibodies directed against HIP. Using immunofluorescence, Rohde et al. (1996) demonstrated that HIP is expressed in both luminal and glandular epithelium of normal human endometrium.MAPPING
Garcia-Barcelo et al. (1997) used a PCR-based strategy to distinguish the functional intron-containing gene RPL29 from multiple pseudogenes. By somatic cell hybrid analysis, radiation hybrid mapping, and fluorescence in situ hybridization, they localized RPL29 to the telomeric region of 3q, where it was the most distal marker identified to that time. The gene is close to RPL35A (180468), which maps to 3q29-qter. Kirn-Safran et al. (2000) mapped the single-copy mouse Rpl29 gene to distal chromosome 9. Promoter analysis indicated the presence of binding motifs for ubiquitously expressed transcription factors and for nuclear factor kappa-B (NFKB; see 164011), as well as the lack of a TATA box. ... More on the omim web site
Dec. 9, 2018: Protein entry updated
Automatic update: model status changed
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).
Oct. 19, 2018: Protein entry updated
Automatic update: OMIM entry 601832 was added.