Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PPP1CB)
The protein contains 327 amino acids for an estimated molecular weight of 37187 Da.
Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). (updated: April 1, 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.
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.
This protein is annotated as membranous in Gene Ontology.
Biological Process
Cell cycle
Cell division
Circadian regulation of gene expression
Entrainment of circadian clock by photoperiod
G2/M transition of mitotic cell cycle
Glycogen metabolic process
MAPK cascade
Mitotic cell cycle
Negative regulation of transforming growth factor beta receptor signaling pathway
Protein dephosphorylation
Regulation of cell adhesion
Regulation of circadian rhythm
Regulation of glycogen biosynthetic process
Regulation of glycogen catabolic process
Small molecule metabolic process
Transforming growth factor beta receptor signaling pathway
Triglyceride catabolic process
The reference OMIM entry for this protein is 600590
Protein phosphatase 1, catalytic subunit, beta isoform; ppp1cb
Protein phosphatase 1-beta
Protein phosphatase 1, catalytic subunit, delta isoform; ppp1cd
Protein phosphatase 1-delta
DESCRIPTION
Protein phosphatase-1 (PP1) is 1 of 4 major serine/threonine-specific protein phosphatases involved in the dephosphorylation of a variety of proteins. These enzymes work in opposition to the protein kinases to control the level of phosphorylation. PP1 has 3 catalytic subunits, designated alpha (176875), beta, and gamma (176914). PP1-beta is also referred to as PP1-delta.CLONING
Barker et al. (1994) isolated a cDNA for PP1-beta (symbolized PPP1CB) from a teratocarcinoma library. Three different PPP1CB mRNAs were seen on Northern blots corresponding to alternate splicing variants. The 3-prime noncoding region of PPP1CB was approximately 90% conserved between man and rodents, suggesting that this region may have functional importance.MAPPING
Barker et al. (1994) assigned the gene for human PPP1CB to chromosome 2 using somatic cell hybrid DNAs and further localized it to 2p23 by fluorescence in situ hybridization. Saadat et al. (1994) confirmed the human map position as 2p23 and showed that rodent homologs mapped to rat 6q21-q23 and mouse 12D. ... 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
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 600590 was added.