Serine/threonine-protein phosphatase 6 regulatory subunit 1 (PPP6R1)
The protein contains 881 amino acids for an estimated molecular weight of 96724 Da.
Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha. (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.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- 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.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- 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.
(right-click above to access to more options from the contextual menu)
The reference OMIM entry for this protein is 610875
Saps domain family, member 1; saps1
Protein phosphatase 6, regulatory subunit 1; pp6r1
Kiaa1115
DESCRIPTION
Protein phosphatase regulatory subunits, such as SAPS1, modulate the activity of protein phosphatase catalytic subunits by restricting substrate specificity, recruiting substrates, and determining the intracellular localization of the holoenzyme. SAPS1 is a regulatory subunit for the protein phosphatase-6 catalytic subunit (PPP6C; 612725) (Stefansson and Brautigan, 2006).CLONING
By sequencing clones obtained from a size-fractionated brain cDNA library, Kikuno et al. (1999) cloned SAPS1, which they designated KIAA1115. The transcript contains a repetitive element in its 5-prime end, and the deduced protein contains 754 amino acids. RT-PCR ELISA detected moderate to high expression in all adult and fetal tissues examined, with highest levels in heart, brain, lung, testis, and ovary. Moderate to high expression was also detected in all brain regions examined. By searching databases for sequences similar to yeast Sap155, Sap185, and Sap190, Stefansson and Brautigan (2006) identified SAPS1, which they called PP6R1. The deduced 829-amino acid protein has a central alpha-helical SAPS domain of about 400 amino acids. Northern blot analysis detected a 4-kb transcript that was highly expressed in testis and moderately expressed in all other tissues examined. Western blot analysis of fractionated HeLa and HEK293 cells showed PP6R1 in the cytosolic fraction.GENE FUNCTION
Using coimmunoprecipitation and protein pull-down assays, Stefansson and Brautigan (2006) showed that epitope-tagged PP6R1 bound endogenous PPP6C, but not PPP2CA (176915). The SAPS domain of PP6R1 was sufficient for its association with PPP6C. Immunoprecipitates containing PPP6C and PP6R1 showed phosphatase activity against a test protein, and the activity was inhibited by okadaic acid, a serine/threonine phosphatase inhibitor. Stefansson and Brautigan (2006) found that PP6R1 and PPP6C associated with I-kappa-B-epsilon (IKBE, or NFKBIE; 604548) in HeLa cells, and knockdown of PP6R1 enhanced degradation of endogenous IKBE in response to TNF-alpha (191160). PP6R1 did not interact with epitope-tagged IKBA (NFKBIA; 164008) or IKBB (NFKBIB; 604495).MAPPING
By radiation hybrid analysis, Kikuno et al. (1999) mapped the SAPS1 gene to chromosome 19. ... More on the omim web site
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 610875 was added.