Ribonucleases P/MRP protein subunit POP1 (POP1)
The protein contains 1024 amino acids for an estimated molecular weight of 114709 Da.
Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends (PubMed:8918471, PubMed:30454648). Also a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences (PubMed:28115465). (updated: May 8, 2019)
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.
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Biological Process
RNA phosphodiester bond hydrolysis, endonucleolytic
TRNA 5'-leader removal
TRNA catabolic process
TRNA processing
Cellular Component
Extracellular space
Multimeric ribonuclease P complex
Nucleolar ribonuclease P complex
Nucleolus
Nucleoplasm
Ribonuclease MRP complex
Molecular Function
Ribonuclease MRP activity
Ribonuclease P activity
Ribonuclease P RNA binding
RNA binding
The reference OMIM entry for this protein is 602486
Processing of precursor 1, s. cerevisiae, homolog of; pop1
CLONING
Lygerou et al. (1994) demonstrated that an S. cerevisiae gene, designated POP1 for 'processing of precursor RNAs,' encodes a protein component of both RNase P and RNase MRP. RNase P and RNase MRP are 2 small nuclear ribonucleoproteins (snRNPs) that have demonstrated enzymatic activity on RNA substrates in vitro. Mutations in yeast POP1 are lethal. Lygerou et al. (1996) identified a human EST with homology to yeast POP1. Human POP1 encodes a predicted 1,024-amino acid protein that has a pI of 9.86. On Northern blots, human POP1 is expressed as a major 4.1-kb and a minor 6-kb transcript, perhaps due to alternative polyadenylation signals. Anti-POP1 antibodies recognize a doublet of approximately 115 kD on Western blots. In HeLa cells, human POP1 localizes to the nucleus and strongly accumulates in the nucleolus.GENE FUNCTION
Lygerou et al. (1996) performed coimmunoprecipitation studies showing that POP1 is associated with both RNase P and RNase MRP snRNAs, and with RNase P enzymatic activity. Lygerou et al. (1996) found that approximately 50% of Th autoimmune sera recognized POP1.MAPPING
Schmiedeknecht et al. (1997) found that p14.5 (602487) and human POP1 are oriented head-to-head, separated by a 102-bp region that contains a bidirectional promoter. Schmiedeknecht et al. (1997) mapped the human POP1 gene to 8q22 using fluorescence in situ hybridization. ... More on the omim web site
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 602486 was added.
May 11, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).