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Protein

cAMP-dependent protein kinase regulatory subunit

Gene

BCY1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory subunit of the cyclic AMP-dependent protein kinase (PKA), an effector of the Ras/cAMP pathway. Inhibits PKA activity in the absence of cAMP. cAMP activates PKA and promotes growth and proliferation in response to good nutrient conditions. Together with ZDS1, provides a negative feedback control on the cell wall integrity-signaling pathway by acting as a negative regulator of MAP kinase SLT2/MPK1.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei249cAMP 11 Publication1
Binding sitei258cAMP 11 Publication1
Binding sitei368cAMP 21 Publication1
Binding sitei377cAMP 21 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi184 – 301cAMP 11 PublicationAdd BLAST118
Nucleotide bindingi302 – 416cAMP 21 PublicationAdd BLAST115

GO - Molecular functioni

GO - Biological processi

  • negative regulation of Ras protein signal transduction Source: SGD
  • positive regulation of adenylate cyclase activity Source: SGD
  • protein localization to bud neck Source: SGD
Complete GO annotation...

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31305-MONOMER.
ReactomeiR-SCE-163615. PKA activation.
R-SCE-164378. PKA activation in glucagon signalling.
R-SCE-180024. DARPP-32 events.
R-SCE-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-SCE-5610787. Hedgehog 'off' state.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase regulatory subunit
Short name:
cAPK regulatory subunit
Alternative name(s):
Bypass of cyclase mutations protein 1
Protein kinase A regulatory subunit
Short name:
PKA regulatory subunit
Gene namesi
Name:BCY1
Synonyms:REG1, SRA1
Ordered Locus Names:YIL033C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIL033C.
SGDiS000001295. BCY1.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: Cytoplasmic when phosphorylated. Nuclear when not phosphorylated.

GO - Cellular componenti

  • cAMP-dependent protein kinase complex Source: InterPro
  • cytoplasm Source: SGD
  • nuclear chromatin Source: SGD
  • nucleus Source: SGD
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi129T → D: Confers increased sensitivity to rapamycin and enhanced accumulation of glycogen upon TORC1 inhibition. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved3 Publications
ChainiPRO_00002054182 – 416cAMP-dependent protein kinase regulatory subunitAdd BLAST415

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3PhosphoserineCurated1
Modified residuei4PhosphoserineCurated1
Modified residuei9PhosphoserineCurated1
Modified residuei68Phosphoserine1 Publication1
Modified residuei70Phosphoserine1 Publication1
Modified residuei74Phosphoserine1 Publication1
Modified residuei77Phosphoserine1 Publication1
Modified residuei79Phosphoserine1 Publication1
Modified residuei81Phosphoserine1 Publication1
Modified residuei83PhosphoserineCombined sources1 Publication1
Modified residuei84Phosphoserine1 Publication1
Modified residuei129Phosphothreonine1 Publication1
Modified residuei130Phosphoserine1 Publication1
Modified residuei131Phosphothreonine1 Publication1
Modified residuei144Phosphothreonine1 Publication1
Modified residuei145Phosphoserine; by autocatalysisCombined sources2 Publications1
Modified residuei147Phosphoserine1 Publication1
Modified residuei150PhosphothreonineCombined sources1 Publication1
Modified residuei160Phosphothreonine1 Publication1

Post-translational modificationi

Phosphorylated by YAK1 in response to glucose starvation. Phosphorylated by MCK1 at Thr-129 upon TOR complex 1 (TORC1) inhibition. Thr-129 phosphorylation activates BCY1 to inhibit PKA. TORC1 inhibits phosphorylation of RxxS/T sites but has no effect on Ser-145 phosphorylation. The phosphorylation sites can be clustered in several groups, all localized in the N-terminal part. The first cluster termed cluster I (CI) is located close to the N-terminus and includes Ser-3, Ser-4 and Ser-9 (PubMed:11134339, PubMed:12704202). The second includes Ser-68, Ser-70, Ser-74, Ser-77, Ser-79, Ser-81, Ser-83, and Ser-84. This cluster of phosphorylation sites, termed cluster II (CII), is important for BCY1 cytoplasmic localization and function (PubMed:11134339, PubMed:12704202, PubMed:20702584). The third cluster of phosphorylated residues consists of Thr-144, Ser-145, Ser-147, Thr-150, and Thr-160. This cluster falls within or near the so-called autoinhibitory domain where the catalytic subunit of PKA autophosphorylates the highly conserved Ser-145 to inhibit BCY1 (PubMed:20702584). A last cluster of phosphorylated residues included Thr-129, Ser-130, and Thr-131 and is termed cluster III (CIII). Sites in CIII (and to a lesser extent in CII) are hyperphosphorylated in response to rapamycin (PubMed:20702584).3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP07278.
PRIDEiP07278.
TopDownProteomicsiP07278.

PTM databases

iPTMnetiP07278.

Interactioni

Subunit structurei

The inactive holoenzyme of cAMP-dependent protein kinase is a tetramer, composed of 2 regulatory subunits (R, encoded by BCY1) and two catalytic subunits (C, encoded by the 3 partially redundant TPK1, TPK2, and TPK3 genes). Activation by cAMP causes dissociation of the holoenzyme, producing 2 active catalytic monomers C and a regulatory dimer R2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-9475,EBI-9475
TPK1P062445EBI-9475,EBI-9458
TPK2P062457EBI-9475,EBI-9465
TPK3P059864EBI-9475,EBI-9470

Protein-protein interaction databases

BioGridi34957. 249 interactors.
DIPiDIP-551N.
IntActiP07278. 17 interactors.
MINTiMINT-411181.

Structurei

Secondary structure

1416
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi173 – 180Combined sources8
Turni183 – 187Combined sources5
Helixi190 – 197Combined sources8
Beta strandi201 – 205Combined sources5
Beta strandi210 – 212Combined sources3
Beta strandi220 – 226Combined sources7
Beta strandi229 – 233Combined sources5
Beta strandi239 – 241Combined sources3
Helixi249 – 254Combined sources6
Beta strandi259 – 266Combined sources8
Beta strandi268 – 274Combined sources7
Helixi275 – 280Combined sources6
Turni281 – 286Combined sources6
Helixi288 – 292Combined sources5
Helixi294 – 299Combined sources6
Helixi301 – 303Combined sources3
Helixi308 – 316Combined sources9
Beta strandi319 – 323Combined sources5
Beta strandi328 – 330Combined sources3
Beta strandi338 – 344Combined sources7
Beta strandi346 – 351Combined sources6
Turni352 – 354Combined sources3
Beta strandi355 – 361Combined sources7
Helixi368 – 373Combined sources6
Beta strandi378 – 385Combined sources8
Beta strandi387 – 393Combined sources7
Helixi394 – 400Combined sources7
Turni402 – 404Combined sources3
Helixi405 – 410Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OF1X-ray2.21A171-416[»]
ProteinModelPortaliP07278.
SMRiP07278.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 183Dimerization and phosphorylationAdd BLAST182
Regioni8 – 45Dimerization/docking domain (D/D)Add BLAST38

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi142 – 146Inhibitor sequence (IS)5

Domaini

The inhibitor sequence (IS) is a substrate recognition motif that docks to the active site cleft of the catalytic subunit rendering the holoenzyme inactive.
Binding of cAMP to the 2 tandem cyclic-nucleotide binding domains (CNB-A and CNB-B) induces a conformational change in BCY1, causing the interaction surface with the catalytic subunit to be destroyed and eventually the dissociation of the R dimer from the C subunits.

Sequence similaritiesi

Contains 2 cyclic nucleotide-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196669.
InParanoidiP07278.
KOiK04739.
OMAiGDPGHSF.
OrthoDBiEOG092C3TMX.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR012198. cAMP_dep_PK_reg_su.
IPR003117. cAMP_dep_PK_reg_su_I/II_a/b.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
SMARTiSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 2 hits.
PROSITEiPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07278-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSSLPKESQ AELQLFQNEI NAANPSDFLQ FSANYFNKRL EQQRAFLKAR
60 70 80 90 100
EPEFKAKNIV LFPEPEESFS RPQSAQSQSR SRSSVMFKSP FVNEDPHSNV
110 120 130 140 150
FKSGFNLDPH EQDTHQQAQE EQQHTREKTS TPPLPMHFNA QRRTSVSGET
160 170 180 190 200
LQPNNFDDWT PDHYKEKSEQ QLQRLEKSIR NNFLFNKLDS DSKRLVINCL
210 220 230 240 250
EEKSVPKGAT IIKQGDQGDY FYVVEKGTVD FYVNDNKVNS SGPGSSFGEL
260 270 280 290 300
ALMYNSPRAA TVVATSDCLL WALDRLTFRK ILLGSSFKKR LMYDDLLKSM
310 320 330 340 350
PVLKSLTTYD RAKLADALDT KIYQPGETII REGDQGENFY LIEYGAVDVS
360 370 380 390 400
KKGQGVINKL KDHDYFGEVA LLNDLPRQAT VTATKRTKVA TLGKSGFQRL
410
LGPAVDVLKL NDPTRH
Length:416
Mass (Da):47,219
Last modified:January 23, 2007 - v4
Checksum:i6D7D97D8E4340AF3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti264A → P in CAA28726 (PubMed:3547325).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15756 Genomic DNA. Translation: AAA34468.1.
M17223 Genomic DNA. Translation: AAA66934.1.
X05051 Genomic DNA. Translation: CAA28726.1.
Z46861 Genomic DNA. Translation: CAA86918.1.
AY558087 Genomic DNA. Translation: AAS56413.1.
BK006942 Genomic DNA. Translation: DAA08515.1.
PIRiA25868. OKBYRC.
RefSeqiNP_012231.1. NM_001179383.1.

Genome annotation databases

EnsemblFungiiYIL033C; YIL033C; YIL033C.
GeneIDi854778.
KEGGisce:YIL033C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15756 Genomic DNA. Translation: AAA34468.1.
M17223 Genomic DNA. Translation: AAA66934.1.
X05051 Genomic DNA. Translation: CAA28726.1.
Z46861 Genomic DNA. Translation: CAA86918.1.
AY558087 Genomic DNA. Translation: AAS56413.1.
BK006942 Genomic DNA. Translation: DAA08515.1.
PIRiA25868. OKBYRC.
RefSeqiNP_012231.1. NM_001179383.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OF1X-ray2.21A171-416[»]
ProteinModelPortaliP07278.
SMRiP07278.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34957. 249 interactors.
DIPiDIP-551N.
IntActiP07278. 17 interactors.
MINTiMINT-411181.

PTM databases

iPTMnetiP07278.

Proteomic databases

MaxQBiP07278.
PRIDEiP07278.
TopDownProteomicsiP07278.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL033C; YIL033C; YIL033C.
GeneIDi854778.
KEGGisce:YIL033C.

Organism-specific databases

EuPathDBiFungiDB:YIL033C.
SGDiS000001295. BCY1.

Phylogenomic databases

GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196669.
InParanoidiP07278.
KOiK04739.
OMAiGDPGHSF.
OrthoDBiEOG092C3TMX.

Enzyme and pathway databases

BioCyciYEAST:G3O-31305-MONOMER.
ReactomeiR-SCE-163615. PKA activation.
R-SCE-164378. PKA activation in glucagon signalling.
R-SCE-180024. DARPP-32 events.
R-SCE-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-SCE-5610787. Hedgehog 'off' state.

Miscellaneous databases

PROiP07278.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR012198. cAMP_dep_PK_reg_su.
IPR003117. cAMP_dep_PK_reg_su_I/II_a/b.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
SMARTiSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 2 hits.
PROSITEiPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKAPR_YEAST
AccessioniPrimary (citable) accession number: P07278
Secondary accession number(s): D6VVP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 171 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4280 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.