Heme-binding protein 2 (HEBP2)
The protein contains 205 amino acids for an estimated molecular weight of 22875 Da.
Can promote mitochondrial permeability transition and facilitate necrotic cell death under different types of stress conditions. (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- 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.
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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| Variant | Description |
|---|---|
| dbSNP:rs3734303 | |
| dbSNP:rs14812 |
No binding partner found
Biological Process
Negative regulation of mitochondrial membrane potential
Neutrophil degranulation
Positive regulation of mitochondrial membrane permeability
Positive regulation of necrotic cell death
Cellular Component
Azurophil granule lumen
Cytoplasm
Extracellular exosome
Extracellular region
Mitochondrion
The reference OMIM entry for this protein is 605825
Heme-binding protein 2; hebp2
Chromosome 6 open reading frame 34; c6orf34
Soul, chicken, homolog of; soul
CLONING
Using 2-tissue subtractive hybridization to identify differentially expressed genes between tissues of interest (the tester) and a control tissue (the driver), followed by suppression PCR to amplify transcripts expressed in both tester tissues, and 5-prime RACE, Zylka and Reppert (1999) identified a cDNA encoding a chicken protein they designated Soul. Northern blot and RT-PCR analysis revealed high expression of 3.0- and 4.0-kb Soul transcripts, which result from alternative splicing, in pineal gland, with somewhat lower expression in retina and no expression in other tissues. The authors named the gene Soul because of the high expression in pineal gland, the organ Rene Descartes hypothesized to be the location of the soul. By EST database searching for homologs of chicken Soul, Zylka and Reppert (1999) identified mouse and human cDNAs encoding heme-binding protein (HBP; 605826) and SOUL. Sequence analysis predicted that the 205-amino acid human SOUL protein, which is 80% identical to the mouse sequence, does not contain a conserved hydrophobic heme-binding region like that found in HBP. Northern blot analysis detected a 1.5-kb Soul transcript in mouse eye. Confocal microscopy demonstrated that expression of mouse Soul is predominantly cytoplasmic with some perinuclear localization. Using the SEC1 homology domain of LRPPRC (607544) as bait in a yeast 2-hybrid screen, Liu and McKeehan (2002) cloned HEBP2 from a liver cDNA library. They also identified a variant, resulting from exon skipping, that contains a deletion of amino acids 12 to 36. HEBP2 shares sequence and structural similarity with a bacterial transcription factor. Northern blot analysis revealed ubiquitous expression of a 1-kb transcript, with highest levels in heart, skeletal muscle, kidney, and liver, intermediate levels in brain, colon, small intestine, placenta, lung, and peripheral blood leukocytes, and lowest levels in thymus and spleen.MAPPING
Scott (2001) mapped the SOUL gene to chromosome 6q24 based on sequence similarity between the SOUL sequence (GenBank GENBANK AF117616) and a chromosome 6 clone (GenBank GENBANK AL031003). ... More on the omim web site
Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 605825 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).