Protein shisa-5 (SHISA5)
The protein contains 240 amino acids for an estimated molecular weight of 25582 Da.
Can induce apoptosis in a caspase-dependent manner and plays a role in p53/TP53-dependent apoptosis. (updated: Oct. 1, 2002)
Protein identification was indicated in the following studies:
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.
This protein is predicted to be membranous by TOPCONS.
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| Variant | Description |
|---|---|
| dbSNP:rs35750010 |
No binding partner found
Biological Process
Cellular protein metabolic process
Intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator
Positive regulation of I-kappaB kinase/NF-kappaB signaling
Post-translational protein modification
The reference OMIM entry for this protein is 607290
Shisa, xenopus, homolog of, 5; shisa5
Scotin
CLONING
Zhang et al. (2000) cloned a cDNA encoding Scotin, which they called HSPC217, from CD34 (142230)-positive hematopoietic stem/progenitor cells. The deduced 170-amino acid protein contains an MYB (189990) DNA-binding domain repeat signature. Microarray analysis of 5 hematopoietic cell lines detected low-level expression of Scotin in NB4 and Jurkat cells, but no expression was detected in HL60, K562, and U937 cells. Bourdon et al. (2002) identified mouse Scotin by differential display of spleen and thymus of normal and p53 (191170) null mice after gamma irradiation of whole animals. The induced 1.85-kb transcript encodes a deduced 235-amino acid protein. By searching an EST database using the mouse sequence as probe, followed by 5-prime and 3-prime RACE, Bourdon et al. (2002) cloned a full-length cDNA encoding Scotin from a placenta cDNA library. The deduced 240-amino acid human protein shares 70% identity with mouse Scotin. Both the human and the mouse proteins contain an N-terminal signal sequence, a central transmembrane domain composed of 18 hydrophobic amino acids, and a proline/tyrosine domain, and both show an apparent molecular mass of 25 kD by Western blot analysis. Immunolocalization of exogenously expressed Scotin revealed colocalization with endoplasmic reticulum (ER) markers. By mutation analysis, Bourdon et al. (2002) determined that the proline-rich domain is required for ER localization.GENE FUNCTION
Bourdon et al. (2002) noted that mouse thymus and spleen cells underwent massive p53-dependent apoptosis following ultraviolet irradiation or exposure to actinomycin D. They found that Scotin mRNA was induced coincident with apoptosis and was expressed only in spleen and thymus of irradiated wildtype mice and not in the spleen or thymus of irradiated p53 null mice. Using electrophoretic mobility shift assays, they confirmed direct binding between p53 and Scotin, and using a luciferase reporter plasmid driven by the mouse Scotin promoter, they confirmed dose-dependent p53 transactiviation. Furthermore, Bourdon et al. (2002) showed that the apoptosis induced by the p53/Scotin pathway is caspase dependent.GENE STRUCTURE
By genomic sequence analysis, Bourdon et al. (2002) determined that the human Scotin gene contains 6 exons. They identified a p53-responsive element of 9 decamers within the mouse Scotin promoter.MAPPING
By radiation hybrid analysis, Zhang et al. (2000) mapped the human Scotin gene to chromosome 3. By genomic sequence analysis, Bourdon et al. (2002) mapped the Scotin gene to chromosome 3p21.3. They also identified a Scotin pseudogene on chromosome Xq13.1-q13.3. ... More on the omim web site
Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 607290 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).