P07278
Gene name |
BCY1 (REG1, SRA1, YIL033C) |
Protein name |
cAMP-dependent protein kinase regulatory subunit |
Names |
cAPK regulatory subunit , Bypass of cyclase mutations protein 1 , Protein kinase A regulatory subunit , PKA regulatory subunit |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YIL033C |
EC number |
|
Protein Class |
|

Descriptions
Autoinhibitory domains (AIDs)
Target domain |
184-300 (Cyclic nucleotide-binding domain) |
Relief mechanism |
Ligand binding |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure

Activated structure

3 structures for P07278
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
3OF1 | X-ray | 221 A | A | 171-416 | PDB |
6XQK | X-ray | 256 A | A/B/C/D/E/F/G/H | 1-50 | PDB |
AF-P07278-F1 | Predicted | AlphaFoldDB |
1 variants for P07278
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
s09-291058 | 204 | S>F | No | SGRP |
No associated diseases with P07278
7 regional properties for P07278
Type | Name | Position | InterPro Accession |
---|---|---|---|
domain | Cyclic nucleotide-binding domain | 184 - 300 | IPR000595-1 |
domain | Cyclic nucleotide-binding domain | 302 - 416 | IPR000595-2 |
domain | cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain | 7 - 45 | IPR003117 |
conserved_site | Cyclic nucleotide-binding, conserved site | 211 - 227 | IPR018488-1 |
conserved_site | Cyclic nucleotide-binding, conserved site | 247 - 264 | IPR018488-2 |
conserved_site | Cyclic nucleotide-binding, conserved site | 329 - 345 | IPR018488-3 |
conserved_site | Cyclic nucleotide-binding, conserved site | 366 - 383 | IPR018488-4 |
6 GO annotations of cellular component
Name | Definition |
---|---|
cAMP-dependent protein kinase complex | An enzyme complex, composed of regulatory and catalytic subunits, that catalyzes protein phosphorylation. Inactive forms of the enzyme have two regulatory chains and two catalytic chains; activation by cAMP produces two active catalytic monomers and a regulatory dimer. |
chromatin | The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome. |
cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
4 GO annotations of molecular function
Name | Definition |
---|---|
cAMP binding | Binding to cAMP, the nucleotide cyclic AMP (adenosine 3',5'-cyclophosphate). |
cAMP-dependent protein kinase inhibitor activity | Binds to and stops, prevents or reduces the activity of a cAMP-dependent protein kinase. |
identical protein binding | Binding to an identical protein or proteins. |
protein kinase A catalytic subunit binding | Binding to one or both of the catalytic subunits of protein kinase A. |
5 GO annotations of biological process
Name | Definition |
---|---|
negative regulation of Ras protein signal transduction | Any process that stops, prevents, or reduces the frequency, rate or extent of Ras protein signal transduction. |
positive regulation of transcription by RNA polymerase II | Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter. |
protein localization to bud neck | A process in which a protein is transported to, or maintained at, a location within a cellular bud neck. |
regulation of cytoplasmic mRNA processing body assembly | Any process that modulates the rate, frequency, or extent of the aggregation, arrangement and bonding together of proteins and RNA molecules to form a cytoplasmic mRNA processing body. |
regulation of protein phosphorylation | Any process that modulates the frequency, rate or extent of addition of phosphate groups into an amino acid in a protein. |
8 homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
P00515 | PRKAR2A | cAMP-dependent protein kinase type II-alpha regulatory subunit | Bos taurus (Bovine) | EV |
P81900 | Pka-R2 | cAMP-dependent protein kinase type II regulatory subunit | Drosophila melanogaster (Fruit fly) | PR |
P31323 | PRKAR2B | cAMP-dependent protein kinase type II-beta regulatory subunit | Homo sapiens (Human) | PR |
P13861 | PRKAR2A | cAMP-dependent protein kinase type II-alpha regulatory subunit | Homo sapiens (Human) | PR |
P31324 | Prkar2b | cAMP-dependent protein kinase type II-beta regulatory subunit | Mus musculus (Mouse) | PR |
P12367 | Prkar2a | cAMP-dependent protein kinase type II-alpha regulatory subunit | Mus musculus (Mouse) | PR |
P12369 | Prkar2b | cAMP-dependent protein kinase type II-beta regulatory subunit | Rattus norvegicus (Rat) | PR |
P12368 | Prkar2a | cAMP-dependent protein kinase type II-alpha regulatory subunit | Rattus norvegicus (Rat) | PR |
10 | 20 | 30 | 40 | 50 | 60 |
MVSSLPKESQ | AELQLFQNEI | NAANPSDFLQ | FSANYFNKRL | EQQRAFLKAR | EPEFKAKNIV |
70 | 80 | 90 | 100 | 110 | 120 |
LFPEPEESFS | RPQSAQSQSR | SRSSVMFKSP | FVNEDPHSNV | FKSGFNLDPH | EQDTHQQAQE |
130 | 140 | 150 | 160 | 170 | 180 |
EQQHTREKTS | TPPLPMHFNA | QRRTSVSGET | LQPNNFDDWT | PDHYKEKSEQ | QLQRLEKSIR |
190 | 200 | 210 | 220 | 230 | 240 |
NNFLFNKLDS | DSKRLVINCL | EEKSVPKGAT | IIKQGDQGDY | FYVVEKGTVD | FYVNDNKVNS |
250 | 260 | 270 | 280 | 290 | 300 |
SGPGSSFGEL | ALMYNSPRAA | TVVATSDCLL | WALDRLTFRK | ILLGSSFKKR | LMYDDLLKSM |
310 | 320 | 330 | 340 | 350 | 360 |
PVLKSLTTYD | RAKLADALDT | KIYQPGETII | REGDQGENFY | LIEYGAVDVS | KKGQGVINKL |
370 | 380 | 390 | 400 | 410 | |
KDHDYFGEVA | LLNDLPRQAT | VTATKRTKVA | TLGKSGFQRL | LGPAVDVLKL | NDPTRH |