EzCatDB: T00255
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DB codeT00255
CATH domainDomain 11.20.890.10 : cAMP-dependent Protein Kinase, Chain A
Domain 22.60.120.10 : Jelly Rolls
Domain 32.60.120.10 : Jelly Rolls
E.C.2.7.11.11

CATH domainRelated DB codes (homologues)
2.60.120.10 : Jelly RollsS00145,S00155,D00842,D00843,M00216,T00101

Enzyme Name
UniProtKBKEGG

P05132P00517Q9DBC7P12849P12367P31324P00514P00515P31322
Protein namecAMP-dependent protein kinase catalytic subunit alphacAMP-dependent protein kinase catalytic subunit alphacAMP-dependent protein kinase type I-alpha regulatory subunitcAMP-dependent protein kinase type I-beta regulatory subunitcAMP-dependent protein kinase type II-alpha regulatory subunitcAMP-dependent protein kinase type II-beta regulatory subunitcAMP-dependent protein kinase type I-alpha regulatory subunitcAMP-dependent protein kinase type II-alpha regulatory subunitcAMP-dependent protein kinase type II-beta regulatory subunitcAMP-dependent protein kinase
PKA
PKA C
protein kinase A
STK22
SynonymsPKA C-alpha
EC 2.7.11.11
PKA C-alpha
EC 2.7.11.11
NoneNoneNoneNoneNoneNoneNone
ContainsNoneNonecAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed
NoneNoneNonecAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed
NoneNone
RefSeqNP_001264827.1 (Protein)
NM_001277898.1 (DNA/RNA sequence)
NP_032880.1 (Protein)
NM_008854.5 (DNA/RNA sequence)
NP_777009.1 (Protein)
NM_174584.2 (DNA/RNA sequence)
NP_068680.1 (Protein)
NM_021880.2 (DNA/RNA sequence)
NP_001240819.1 (Protein)
NM_001253890.1 (DNA/RNA sequence)
NP_032949.3 (Protein)
NM_008923.3 (DNA/RNA sequence)

NP_035288.2 (Protein)
NM_011158.3 (DNA/RNA sequence)
NP_001069826.1 (Protein)
NM_001076358.1 (DNA/RNA sequence)
NP_001178296.1 (Protein)
NM_001191367.1 (DNA/RNA sequence)
NP_777074.1 (Protein)
NM_174649.2 (DNA/RNA sequence)
PfamPF00069 (Pkinase)
[Graphical view]
PF00069 (Pkinase)
[Graphical view]
PF00027 (cNMP_binding)
PF02197 (RIIa)
[Graphical view]
PF00027 (cNMP_binding)
PF02197 (RIIa)
[Graphical view]
PF00027 (cNMP_binding)
PF02197 (RIIa)
[Graphical view]
PF00027 (cNMP_binding)
PF02197 (RIIa)
[Graphical view]
PF00027 (cNMP_binding)
PF02197 (RIIa)
[Graphical view]
PF00027 (cNMP_binding)
PF02197 (RIIa)
[Graphical view]
PF00027 (cNMP_binding)
PF02197 (RIIa)
[Graphical view]


UniProtKB:Accession NumberP05132P00517Q9DBC7P12849P12367P31324P00514P00515P31322
Entry nameKAPCA_MOUSEKAPCA_BOVINKAP0_MOUSEKAP1_MOUSEKAP2_MOUSEKAP3_MOUSEKAP0_BOVINKAP2_BOVINKAP3_BOVIN
ActivityATP + a protein = ADP + a phosphoprotein.ATP + a protein = ADP + a phosphoprotein.






SubunitA number of inactive tetrameric holoenzymes are produced by the combination of homo- or heterodimers of the different regulatory subunits associated with two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits.A number of inactive tetrameric holoenzymes are produced by the combination of homo- or heterodimers of the different regulatory subunits associated with two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits.The inactive form of the enzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP produces two active catalytic monomers and a regulatory dimer that binds four cAMP molecules. PRKAR1A also interacts with RFC2, the complex may be involved in cell survival (By similarity). Interacts with AKAP4.The inactive form of the enzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP produces two active catalytic monomers and a regulatory dimer that binds four cAMP molecules.The inactive form of the enzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP produces two active catalytic monomers and a regulatory dimer that binds four cAMP molecules. Interacts with AKAP4. Interacts with CBFA2T3 (By similarity).The inactive form of the enzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP produces two active catalytic monomers and a regulatory dimer that binds four cAMP molecules.The inactive form of the enzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP produces two active catalytic monomers and a regulatory dimer that binds four cAMP molecules. PRKAR1A also interacts with RFC2, the complex may be involved in cell survival. Interacts with AKAP4 (By similarity).The inactive form of the enzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP produces two active catalytic monomers and a regulatory dimer that binds four cAMP molecules. Interacts with AKAP4 and CBFA2T3 (By similarity).The inactive form of the enzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP produces two active catalytic monomers and a regulatory dimer that binds four cAMP molecules.
Subcellular locationCytoplasm (By similarity). Nucleus (By similarity). Note=Translocates into the nucleus (monomeric catalytic subunit) (By similarity). The inactive holoenzyme is found in the cytoplasm (By similarity).Cytoplasm. Nucleus. Note=Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenzyme is found in the cytoplasm.






Cofactor









Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00002C00017C00008C00562
CompoundATPProteinADPPhosphoprotein
Typeamine group,nucleotidepeptide/proteinamine group,nucleotidepeptide/protein,phosphate group/phosphate ion
ChEBI15422

16761

PubChem5957

6022

            
1r2aAUnboundUnboundUnboundUnbound
1r2aBUnboundUnboundUnboundUnbound
1rgsA01UnboundUnboundUnboundUnbound
1rgsA02UnboundUnboundUnboundUnbound

Active-site residues
pdb
        
1r2aA
1r2aB
1rgsA01
1rgsA02


references
[1]
CommentsDISULFIDE BONDS
Medline ID88033069
PubMed ID3667618
JournalJ Biol Chem
Year1987
Volume262
Pages14961-6
AuthorsBubis J, Vedvick TS, Taylor SS
TitleAntiparallel alignment of the two protomers of the regulatory subunit dimer of cAMP-dependent protein kinase I.
Related UniProtKBP00514
[2]
Comments3D-STRUCTURE MODELING
Medline ID87157645
PubMed ID3030405
JournalBiochemistry
Year1987
Volume26
Pages343-51
AuthorsWeber IT, Steitz TA, Bubis J, Taylor SS
TitlePredicted structures of cAMP binding domains of type I and II regulatory subunits of cAMP-dependent protein kinase.
Related UniProtKBP00514
[3]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 113-379
PubMed ID7638597
JournalScience
Year1995
Volume269
Pages807-13
AuthorsSu Y, Dostmann WR, Herberg FW, Durick K, Xuong NH, Ten Eyck L, Taylor SS, Varughese KI
TitleRegulatory subunit of protein kinase A: structure of deletion mutant with cAMP binding domains.
Related PDB1rgs
Related UniProtKBP00514
[4]
PubMed ID7873523
JournalBiochemistry
Year1995
Volume34
Pages2447-54
AuthorsAdams JA, McGlone ML, Gibson R, Taylor SS
TitlePhosphorylation modulates catalytic function and regulation in the cAMP-dependent protein kinase.
[5]
PubMed ID7756252
JournalBiochemistry
Year1995
Volume34
Pages6267-71
AuthorsYang S, Fletcher WH, Johnson DA
TitleRegulation of cAMP-dependent protein kinase: enzyme activation without dissociation.
[6]
PubMed ID8524844
JournalProc Natl Acad Sci U S A
Year1995
Volume92
Pages11761-5
AuthorsLuo K, Zhou P, Lodish HF
TitleThe specificity of the transforming growth factor beta receptor kinases determined by a spatially addressable peptide library.
[7]
PubMed ID8612810
JournalFEBS Lett
Year1996
Volume384
Pages138-42
AuthorsSahara S, Sato K, Kaise H, Mori K, Sato A, Aoto M, Tokmakov AA, Fukami Y
TitleBiochemical evidence for the interaction of regulatory subunit of cAMP-dependent protein kinase with IDA (Inter-DFG-APE) region of catalytic subunit.
[8]
PubMed ID9300482
JournalProtein Sci
Year1997
Volume6
Pages1825-34
AuthorsGibson RM, Ji-Buechler Y, Taylor SS
TitleIdentification of electrostatic interaction sites between the regulatory and catalytic subunits of cyclic AMP-dependent protein kinase.
[9]
PubMed ID9050991
JournalOncogene
Year1997
Volume14
Pages923-8
AuthorsTortora G, Damiano V, Bianco C, Baldassarre G, Bianco AR, Lanfrancone L, Pelicci PG, Ciardiello F
TitleThe RIalpha subunit of protein kinase A (PKA) binds to Grb2 and allows PKA interaction with the activated EGF-receptor.
[10]
PubMed ID9295304
JournalJ Biol Chem
Year1997
Volume272
Pages23637-44
AuthorsNewlon MG, Roy M, Hausken ZE, Scott JD, Jennings PA
TitleThe A-kinase anchoring domain of type IIalpha cAMP-dependent protein kinase is highly helical.
[11]
PubMed ID10485331
JournalMol Cell Biochem
Year1999
Volume197
Pages117-28
AuthorsNikolakaki E, Fissentzidis A, Giannakouros T, Georgatsos JG
TitlePurification and characterization of a dimer form of the cAMP-dependent protein kinase from mouse liver cytosol.
[12]
PubMed ID10026146
JournalJ Biol Chem
Year1999
Volume274
Pages5370-8
AuthorsZimmermann B, Chiorini JA, Ma Y, Kotin RM, Herberg FW
TitlePrKX is a novel catalytic subunit of the cAMP-dependent protein kinase regulated by the regulatory subunit type I.
[13]
CommentsSTRUCTURE BY NMR OF 1-43.
Medline ID99173235
PubMed ID10074940
JournalNat Struct Biol
Year1999
Volume6
Pages222-7
AuthorsNewlon MG, Roy M, Morikis D, Hausken ZE, Coghlan V, Scott JD, Jennings PA
TitleThe molecular basis for protein kinase A anchoring revealed by solution NMR.
Related PDB1r2a
Related UniProtKBP12367
[14]
PubMed ID11206066
JournalProtein Sci
Year2000
Volume9
Pages2446-56
AuthorsMuhonen WW, Shabb JB
TitleResonant mirror biosensor analysis of type Ialpha cAMP-dependent protein kinase B domain--cyclic nucleotide interactions.
[15]
PubMed ID10801316
JournalBiochemistry
Year2000
Volume39
Pages5662-71
AuthorsLeon DA, Canaves JM, Taylor SS
TitleProbing the multidomain structure of the type I regulatory subunit of cAMP-dependent protein kinase using mutational analysis: role and environment of endogenous tryptophans.
[16]
PubMed ID10753751
JournalCurr Biol
Year2000
Volume10
Pages417-20
AuthorsDiviani D, Langeberg LK, Doxsey SJ, Scott JD
TitlePericentrin anchors protein kinase A at the centrosome through a newly identified RII-binding domain.
[17]
PubMed ID10899163
JournalJ Biol Chem
Year2000
Volume275
Pages35146-52
AuthorsBanky P, Newlon MG, Roy M, Garrod S, Taylor SS, Jennings PA
TitleIsoform-specific differences between the type Ialpha and IIalpha cyclic AMP-dependent protein kinase anchoring domains revealed by solution NMR.
[18]
PubMed ID11342137
JournalStructure (Camb)
Year2001
Volume9
Pages73-82
AuthorsDiller TC, Madhusudan, Xuong NH, Taylor SS
TitleMolecular basis for regulatory subunit diversity in cAMP-dependent protein kinase: crystal structure of the type II beta regulatory subunit.
[19]
PubMed ID11593431
JournalOncogene
Year2001
Volume20
Pages6225-32
AuthorsFukuyama T, Sueoka E, Sugio Y, Otsuka T, Niho Y, Akagi K, Kozu T
TitleMTG8 proto-oncoprotein interacts with the regulatory subunit of type II cyclic AMP-dependent protein kinase in lymphocytes.
[20]
PubMed ID12381327
JournalJ Mol Biol
Year2002
Volume323
Pages377-86
AuthorsAnand GS, Hughes CA, Jones JM, Taylor SS, Komives EA
TitleAmide H/2H exchange reveals communication between the cAMP and catalytic subunit-binding sites in the R(I)alpha subunit of protein kinase A.
[21]
PubMed ID11943768
JournalJ Biol Chem
Year2002
Volume277
Pages22902-8
AuthorsDahle MK, Gronning LM, Cederberg A, Blomhoff HK, Miura N, Enerback S, Tasken KA, Tasken K
TitleMechanisms of FOXC2- and FOXD1-mediated regulation of the RI alpha subunit of cAMP-dependent protein kinase include release of transcriptional repression and activation by protein kinase B alpha and cAMP.
[22]
PubMed ID11877433
JournalJ Biol Chem
Year2002
Volume277
Pages16814-22
AuthorsRayner TF, Gray JV, Thorner JW
TitleDirect and novel regulation of cAMP-dependent protein kinase by Mck1p, a yeast glycogen synthase kinase-3.
[23]
PubMed ID11799117
JournalJ Biol Chem
Year2002
Volume277
Pages12423-31
AuthorsTung CS, Walsh DA, Trewhella J
TitleA structural model of the catalytic subunit-regulatory subunit dimeric complex of the cAMP-dependent protein kinase.

comments
The E.C. was transferred from 2.7.1.37 to 2.7.11.11.
This protein is a regulatory subunit. The catalytic subunit is separate from this protein (see D00114; Swiss-prot;P00517). The inactive form of the enzyme is composed of two regulatory subunits and two catalytic subunits. Activation by c-AMP results in the two active catalytic subunits and a regulatory dimer that binds four cAMP molecules. This regulatory subunit has two cAMP-binding sites.
The C-terminal domains of this protein have got the cAMP binding sites. The N-terminal domain seems to be involved in dimerization (PDB;1r2a).

createdupdated
2003-07-162009-03-19


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Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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