RING finger and SPRY domain-containing protein 1 (RSPRY1)
The protein contains 576 amino acids for an estimated molecular weight of 64180 Da.
No function (updated: March 4, 2015)
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.
- 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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| Variant | Description |
|---|---|
| SEMDFA |
The reference OMIM entry for this protein is 616585
Ring finger- and spry domain-containing protein 1; rspry1
Kiaa1972
CLONING
By sequencing clones obtained from a size-fractionated fetal brain cDNA library, Nagase et al. (2001) cloned RSPRY1, which they designated KIAA1972. The deduced 576-amino acid protein has a SPRY domain and a putative C3HC4-type zinc finger domain, suggesting the protein has a function in nucleic acid management. RT-PCR ELISA detected highest KIAA1972 expression in liver, kidney, testis, ovary, and spleen, with moderate expression in spinal cord and fetal liver, and lower expression in all other tissues examined, including adult and fetal brain. Within specific adult brain regions, highest expression was detected in substantia nigra. Faden et al. (2015) examined the expression of Rspry1 transcripts and localization of the encoded protein by in situ hybridization, RT-PCR, and immunohistochemistry in mid- to late-gestation mouse embryos and newborns. Rspry1 transcripts and encoded protein were expressed in and localized to intact mouse limb bud mesenchyme from as early as embryonic day (E) 12.5. At E18.5, coinciding with primary ossification in the mouse, Rspry1 protein was abundantly detected in most developing endochondral bones and in skeletal muscles, as well as in developing heart, kidney, and brain. In the E18.5 forelimb, Rspry1 was detected in the humerus, ulna, radius, carpals, and metacarpals. Rspry1 was also detected in the bones of the E18.5 hindlimb, including the femur, tibia, fibula, tarsals, and metatarsals. Strong localization was detected in both osteoblasts and osteocytes within these bones, with minimal localization in chondrocytes. A second site of prominent Rspry1 bone localization was in the perichondrium and periosteum, with highest levels in the innermost cellular layer. Expression was also detected in embryonic and postnatal brain and in developing craniofacial tissues.MAPPING
Hartz (2015) mapped the RSPRY1 gene to chromosome 16q13 based on an alignment of the RSPRY1 sequence (GenBank GENBANK AB075852) with the genomic sequence (GRCh38).MOLECULAR GENETICS
In affected members of a consanguineous Bedouin Saudi family with spondyloepimetaphyseal dysplasia of the Faden-Alkuraya type (SEMDFA; 616723), Faden et al. (2015) identified homozygosity for a 1-bp duplication in the RSPRY1 gene (616585.0001). Using a gene-centric 'matchmaking' system, Faden et al. (2015) identified a similarly affected Peruvian boy who was homozygous for a missense mutation in RSPRY1 (G41C; 616585.0002). ... More on the omim web site
Feb. 10, 2018: Protein entry updated
Automatic update: OMIM entry 616585 was added.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 25, 2017: Additional information
No protein expression data in P. Mayeux work for RSPRY1