Staphylococcal nuclease domain-containing protein 1 (SND1)
The protein contains 910 amino acids for an estimated molecular weight of 101997 Da.
Endonuclease that mediates miRNA decay of both protein-free and AGO2-loaded miRNAs (PubMed:28546213, PubMed:18453631). As part of its function in miRNA decay, regulates mRNAs involved in G1-to-S phase transition (PubMed:28546213). Functions as a bridging factor between STAT6 and the basal transcription factor (PubMed:12234934). Plays a role in PIM1 regulation of MYB activity (PubMed:9809063). Functions as a transcriptional coactivator for STAT5 (By similarity).', '(Microbial infection) Functions as a transcriptional coactivator for the Epstein-Barr virus nuclear antigen 2 (EBNA2). (updated: Sept. 12, 2018)
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.
- 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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Biological Process
Gene silencing by RNA
MiRNA catabolic process
Osteoblast differentiation
Regulation of cell cycle process
Regulation of transcription, DNA-templated
RNA catabolic process
Transcription, DNA-templated
Viral process
Cellular Component
Cytoplasm
Cytosol
Dense body
Extracellular exosome
Melanosome
Membrane
Mitochondrion
Nucleus
RISC complex
The reference OMIM entry for this protein is 602181
Ebna2 coactivator p100
P100
Staphylococcal nuclease domain-containing protein 1; snd1
CLONING
Epstein-Barr virus (EBV) nuclear antigen-2 (EBNA2) activates transcription of specific genes and is essential for EBV-mediated B-lymphocyte transformation. Tong et al. (1995) showed that EBNA2 binds to the nuclear protein p100 and that p100 coactivates gene expression mediated by the EBNA2 acidic domain. Using affinity cloning, Tong et al. (1995) cloned the human p100 gene and showed that it encodes an 885-amino acid polypeptide that contains 2 potential nuclear localization signals. By Northern blotting, p100 appeared to be ubiquitously expressed. The p100 protein also binds both the p56 and p34 subunits of transcription factor IIE (189962). Callebaut and Mornon (1997) identified a novel domain within the p100 sequence that they named the 'tudor domain' because it is present in multiple copies in the Drosophila 'tudor' protein.GENE FUNCTION
Caudy et al. (2003) demonstrated that Tudor-SN (tudor staphylococcal nuclease), a protein containing 5 staphylococcal/micrococcal nuclease domains and a tudor domain, is a component of the RNA-induced silencing complex (RISC) enzyme in C. elegans, Drosophila, and mammals. Although Tudor-SN contains noncanonical active-site sequences, Caudy et al. (2003) showed that purified Tudor-SN exhibits nuclease activity similar to that of other staphylococcal nucleases. Notably, both purified Tudor-SN and RISC are inhibited by a specific competitive inhibitor of micrococcal nuclease. Tudor-SN is the first RISC subunit to be identified that contains a recognizable nuclease domain, and could therefore contribute to the RNA degradation observed in RNAi.MAPPING
By somatic cell hybrid analysis and FISH, Lienard et al. (2000) mapped the SND1 gene to human chromosome 7q31.3 and rat chromosome 4q23. ... More on the omim web site
Oct. 2, 2018: 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 602181 was added.
Feb. 24, 2016: Protein entry updated
Automatic update: model status changed