cAMP-dependent protein kinase type I-beta regulatory subunit (PRKAR1B)
The protein contains 381 amino acids for an estimated molecular weight of 43073 Da.
Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. (updated: Oct. 10, 2018)
Protein identification was indicated in the following studies:
- 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.
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, is annotated as membranous in UniProt.
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Biological Process
Activation of protein kinase A activity
Blood coagulation
Cellular response to glucagon stimulus
CGMP-mediated signaling
Chemical synaptic transmission
Learning or memory
Modulation of chemical synaptic transmission
Negative regulation of cAMP-dependent protein kinase activity
Negative regulation of inflammatory response to antigenic stimulus
Protein phosphorylation
Regulation of cAMP-mediated signaling
Regulation of protein kinase A signaling
Regulation of synaptic vesicle cycle
Renal water homeostasis
The reference OMIM entry for this protein is 176911
Protein kinase, camp-dependent, regulatory, type i, beta; prkar1b
Prkar1
DESCRIPTION
Cyclic AMP-dependent protein kinase A (PKA) is an essential enzyme in the signaling pathway of the second messenger cAMP. Through phosphorylation of target proteins, PKA controls many biochemical events in the cell including regulation of metabolism, ion transport, and gene transcription. The PKA holoenzyme is composed of 2 regulatory and 2 catalytic subunits and dissociates from the regulatory subunits upon binding of cAMP.MAPPING
Solberg et al. (1992) mapped the gene encoding the regulatory subunit RI-beta (PRKAR1B) to 7p using RFLPs in relation to the CEPH panel of 40 families. A 6-point local framework map including PRKAR1B indicated that this locus is the most distal of the hitherto marked 7p marker loci, the order being as follows: pter--PRKAR1B--D7S21--D7S108--D7S17--D7S149--D7S62--cen. The rate of recombination between PRKAR1B and D7S21 was significantly higher in males than in females. (The same phenomenon has been found for other terminal chromosome regions; see Nakamura et al. (1988, 1989).) As D7S21 has been physically mapped to 7p22 (Royle et al., 1988), mapping data suggested that PRKAR1B is located in the region 7pter-p22.GENE FUNCTION
Danial et al. (2003) undertook a proteomic analysis to assess whether BAD (603167) might participate in mitochondrial physiology. In liver mitochondria, BAD resides in a functional holoenzyme complex together with protein kinase A and protein phosphatase-1 (PP1; see 176875) catalytic units, WAVE1 (605035) as an A kinase-anchoring protein, and glucokinase (138079). Using mitochondria from hepatocytes of Bad-deficient mice, Danial et al. (2003) demonstrated that BAD is required to assemble the complex, the lack of which results in diminished mitochondria-based glucokinase activity and blunted mitochondrial respiration in response to glucose. Glucose deprivation results in dephosphorylation of BAD, and BAD-dependent cell death. ... More on the omim web site
Oct. 19, 2018: Protein entry updated
Automatic update: OMIM entry 176911 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).