Tyrosine-protein phosphatase non-receptor type 23 (PTPN23)
The protein contains 1636 amino acids for an estimated molecular weight of 178974 Da.
Plays a role in sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs) via its interaction with the ESCRT-I complex (endosomal sorting complex required for transport I), and possibly also other ESCRT complexes (PubMed:18434552, PubMed:21757351). May act as a negative regulator of Ras-mediated mitogenic activity (PubMed:18434552). Plays a role in ciliogenesis (PubMed:20393563). (updated: Oct. 16, 2019)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- 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.
- 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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Biological Process
Cellular response to cytokine stimulus
Cilium assembly
Early endosome to late endosome transport
Endocytic recycling
Negative regulation of epithelial cell migration
Peptidyl-tyrosine dephosphorylation
Positive regulation of adherens junction organization
Positive regulation of early endosome to late endosome transport
Positive regulation of homophilic cell adhesion
Positive regulation of Wnt protein secretion
Protein transport
Ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway
The reference OMIM entry for this protein is 606584
Protein-tyrosine phosphatase, nonreceptor-type, 23; ptpn23
His-domain protein-tyrosine phosphatase; hdptp
Kiaa1471
CLONING
Toyooka et al. (2000) isolated a cDNA encoding a novel protein tyrosine phosphatase, PTPN23, from a gastric cancer cell line. The predicted protein contains at least 1,636 amino acids and has several features distinct from those in previously identified PTPs, the most striking of which is the sequence VHCSSG instead of the invariant VHCSAG sequence at the PTP active center. PTPN23 contains a zinc-hand domain, which the authors called a 'His domain' (HD); several SH3-binding motifs; a tyrosine phosphatase domain; a C-terminal PEST motif; and an N-terminal domain similar to yeast BRO1, mouse rhophilin (601031), and human AIP1 (605555). It appears to be the homolog of rat PTP-TD14 which has been found to inhibit activated H-ras-mediated cell transformation (Cao et al., 1998). Northern blot analysis in rat revealed ubiquitous expression of a 6-kb PTPN23 transcript. Expression experiments demonstrated that PTPN23 is distributed within the cytoplasm. In the RERF-LCMA small cell lung cancer cell line (see 182280), Toyooka et al. (2000) identified a hemizygous missense mutation in the PTPN23 gene, a CCT-to-TCT change resulting in a pro1099-to-ser substitution. The mutation causes an alteration in the structure of one of the SH3-binding motifs within the His domain.GENE FUNCTION
In a functional genomic screen using RNA interference, Kim et al. (2010) identified PTPN23 as a gene involved in ciliogenesis control. Silencing of PTPN23 greatly reduced the number of ciliated cells in functional assays.GENE STRUCTURE
Toyooka et al. (2000) determined that the PTPN23 gene contains at least 25 exons.MAPPING
By radiation hybrid analysis and sequence analysis, Toyooka et al. (2000) mapped the PTPN23 gene between markers WI-11814 and WI-18411 on chromosome 3p21.3, within a putative tumor suppressor region. ... More on the omim web site
Oct. 27, 2019: 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
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 606584 was added.