PRKACB

Protein-coding gene in the species Homo sapiens
PRKACB
Identifiers
AliasesPRKACB, PKA C-beta, PKACB, protein kinase cAMP-activated catalytic subunit beta, CAFD2
External IDsOMIM: 176892; MGI: 97594; HomoloGene: 121718; GeneCards: PRKACB; OMA:PRKACB - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for PRKACB
Genomic location for PRKACB
Band1p31.1Start84,078,062 bp[1]
End84,238,498 bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for PRKACB
Genomic location for PRKACB
Band3|3 H2Start146,435,329 bp[2]
End146,518,745 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • endothelial cell

  • Brodmann area 23

  • postcentral gyrus

  • middle temporal gyrus

  • entorhinal cortex

  • orbitofrontal cortex

  • pons

  • Brodmann area 46

  • superior vestibular nucleus

  • corpus callosum
Top expressed in
  • ventromedial nucleus

  • anterior amygdaloid area

  • lateral septal nucleus

  • dorsomedial hypothalamic nucleus

  • mammillary body

  • arcuate nucleus

  • paraventricular nucleus of hypothalamus

  • lateral hypothalamus

  • ventral tegmental area

  • primary motor cortex
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • nucleotide binding
  • protein kinase activity
  • cAMP-dependent protein kinase activity
  • protein binding
  • ATP binding
  • ubiquitin protein ligase binding
  • magnesium ion binding
  • kinase activity
  • protein serine/threonine kinase activity
  • protein kinase A regulatory subunit binding
Cellular component
  • cytoplasm
  • centrosome
  • membrane
  • plasma membrane
  • nucleoplasm
  • ciliary base
  • perinuclear region of cytoplasm
  • cAMP-dependent protein kinase complex
  • extracellular exosome
  • nucleus
  • cytosol
  • intercellular bridge
Biological process
  • negative regulation of meiotic cell cycle
  • activation of protein kinase A activity
  • phosphorylation
  • adenylate cyclase-modulating G protein-coupled receptor signaling pathway
  • cellular response to glucagon stimulus
  • negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning
  • blood coagulation
  • stimulatory C-type lectin receptor signaling pathway
  • regulation of protein processing
  • protein phosphorylation
  • neural tube closure
  • response to clozapine
  • renal water homeostasis
  • signal transduction
  • high-density lipoprotein particle assembly
  • G protein-coupled receptor signaling pathway
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5567

18749

Ensembl

ENSG00000142875

ENSMUSG00000005034

UniProt

P22694

P68181

RefSeq (mRNA)
NM_001242857
NM_001242858
NM_001242859
NM_001242860
NM_001242861

NM_001242862
NM_001300915
NM_001300916
NM_001300917
NM_002731
NM_182948
NM_207578
NM_001375560
NM_001375561
NM_001375562
NM_001375563
NM_001375564
NM_001375565
NM_001375569
NM_001375571
NM_001375572
NM_001375573
NM_001375574
NM_001375575
NM_001375576
NM_001375577
NM_001375578
NM_001375579
NM_001375580
NM_001375581

NM_001164198
NM_001164199
NM_001164200
NM_011100

RefSeq (protein)
NP_001229786
NP_001229787
NP_001229788
NP_001229789
NP_001229790

NP_001229791
NP_001287844
NP_001287845
NP_001287846
NP_002722
NP_891993
NP_997461
NP_001362489
NP_001362490
NP_001362491
NP_001362492
NP_001362493
NP_001362494
NP_001362498
NP_001362500
NP_001362501
NP_001362502
NP_001362503
NP_001362504
NP_001362505
NP_001362506
NP_001362507
NP_001362508
NP_001362509
NP_001362510
NP_002722.1

NP_001157670
NP_001157671
NP_001157672
NP_035230

Location (UCSC)Chr 1: 84.08 – 84.24 MbChr 3: 146.44 – 146.52 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

cAMP-dependent protein kinase catalytic subunit beta is an enzyme that in humans is encoded by the PRKACB gene.[5]

cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the protein kinase A (PKA), which transduces the signal through phosphorylation of different target proteins. The inactive holoenzyme of PKA is a tetramer composed of two regulatory and 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. Four different regulatory subunits and three catalytic subunits of PKA have been identified in humans. The protein encoded by this gene is a member of the serine/threonine protein kinase family and is a catalytic subunit of PKA. Three alternatively spliced transcript variants encoding distinct isoforms have been observed.[5]

Interactions

PRKACB has been shown to interact with Ryanodine receptor 2[6] and Low affinity nerve growth factor receptor.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000142875 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000005034 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: PRKACB protein kinase, cAMP-dependent, catalytic, beta".
  6. ^ Marx SO, Reiken S, Hisamatsu Y, Jayaraman T, Burkhoff D, Rosemblit N, Marks A R (May 2000). "PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts". Cell. 101 (4). UNITED STATES: 365–76. doi:10.1016/S0092-8674(00)80847-8. ISSN 0092-8674. PMID 10830164. S2CID 6496567.
  7. ^ Higuchi H, Yamashita Toshihide, Yoshikawa Hideki, Tohyama Masaya (April 2003). "PKA phosphorylates the p75 receptor and regulates its localization to lipid rafts". EMBO J. 22 (8). England: 1790–800. doi:10.1093/emboj/cdg177. ISSN 0261-4189. PMC 154469. PMID 12682012.

Further reading

  • Simard J, Bérubé D, Sandberg M, et al. (1992). "Assignment of the gene encoding the catalytic subunit C beta of cAMP-dependent protein kinase to the p36 band on chromosome 1". Hum. Genet. 88 (6): 653–7. doi:10.1007/BF02265292. PMID 1551670. S2CID 20799373.
  • Hofmann B, Nishanian P, Baldwin RL, et al. (1991). "HIV inhibits the early steps of lymphocyte activation, including initiation of inositol phospholipid metabolism". J. Immunol. 145 (11): 3699–705. doi:10.4049/jimmunol.145.11.3699. PMID 1978848.
  • Beebe SJ, Oyen O, Sandberg M, et al. (1990). "Molecular cloning of a tissue-specific protein kinase (C gamma) from human testis--representing a third isoform for the catalytic subunit of cAMP-dependent protein kinase". Mol. Endocrinol. 4 (3): 465–75. doi:10.1210/mend-4-3-465. PMID 2342480.
  • Scarpetta MA, Uhler MD (1993). "Evidence for two additional isoforms of the endogenous protein kinase inhibitor of cAMP-dependent protein kinase in mouse". J. Biol. Chem. 268 (15): 10927–31. doi:10.1016/S0021-9258(18)82074-9. PMID 7684369.
  • Hofmann B, Nishanian P, Nguyen T, et al. (1993). "Human immunodeficiency virus proteins induce the inhibitory cAMP/protein kinase A pathway in normal lymphocytes". Proc. Natl. Acad. Sci. U.S.A. 90 (14): 6676–80. Bibcode:1993PNAS...90.6676H. doi:10.1073/pnas.90.14.6676. PMC 46995. PMID 7688126.
  • Hofmann B, Nishanian P, Fan J, et al. (1994). "HIV Gag p17 protein impairs proliferation of normal lymphocytes in vitro". AIDS. 8 (7): 1016–7. doi:10.1097/00002030-199407000-00025. PMID 7946090.
  • Gamm DM, Baude EJ, Uhler MD (1996). "The major catalytic subunit isoforms of cAMP-dependent protein kinase have distinct biochemical properties in vitro and in vivo". J. Biol. Chem. 271 (26): 15736–42. doi:10.1074/jbc.271.26.15736. PMID 8662989.
  • Swingler S, Gallay P, Camaur D, et al. (1997). "The Nef protein of human immunodeficiency virus type 1 enhances serine phosphorylation of the viral matrix". J. Virol. 71 (6): 4372–7. doi:10.1128/JVI.71.6.4372-4377.1997. PMC 191654. PMID 9151826.
  • Chen P, Mayne M, Power C, Nath A (1997). "The Tat protein of HIV-1 induces tumor necrosis factor-alpha production. Implications for HIV-1-associated neurological diseases". J. Biol. Chem. 272 (36): 22385–8. doi:10.1074/jbc.272.36.22385. PMID 9278385.
  • Liapi C, Takahashi N, Raynaud F, et al. (1998). "Effects of [D-Ala1] peptide T-NH2 and HIV envelope glycoprotein gp120 on cyclic AMP dependent protein kinases in normal and psoriatic human fibroblasts". J. Invest. Dermatol. 110 (4): 332–7. doi:10.1046/j.1523-1747.1998.00149.x. PMID 9540970.
  • Rabbi MF, al-Harthi L, Saifuddin M, Roebuck KA (1998). "The cAMP-dependent protein kinase A and protein kinase C-beta pathways synergistically interact to activate HIV-1 transcription in latently infected cells of monocyte/macrophage lineage". Virology. 245 (2): 257–69. doi:10.1006/viro.1998.9158. PMID 9636365.
  • Zidovetzki R, Wang JL, Chen P, et al. (1998). "Human immunodeficiency virus Tat protein induces interleukin 6 mRNA expression in human brain endothelial cells via protein kinase C- and cAMP-dependent protein kinase pathways". AIDS Res. Hum. Retroviruses. 14 (10): 825–33. doi:10.1089/aid.1998.14.825. PMID 9671211.
  • Mayne M, Bratanich AC, Chen P, et al. (1998). "HIV-1 tat molecular diversity and induction of TNF-alpha: implications for HIV-induced neurological disease". Neuroimmunomodulation. 5 (3–4): 184–92. doi:10.1159/000026336. PMID 9730685. S2CID 19529677.
  • Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
  • Jiang CH, Tsien JZ, Schultz PG, Hu Y (2001). "The effects of aging on gene expression in the hypothalamus and cortex of mice". Proc. Natl. Acad. Sci. U.S.A. 98 (4): 1930–4. Bibcode:2001PNAS...98.1930J. doi:10.1073/pnas.98.4.1930. PMC 29359. PMID 11172053.
  • Ørstavik S, Reinton N, Frengen E, et al. (2001). "Identification of novel splice variants of the human catalytic subunit Cbeta of cAMP-dependent protein kinase". Eur. J. Biochem. 268 (19): 5066–73. doi:10.1046/j.0014-2956.2001.02429.x. PMID 11589697.
  • Wu KJ, Mattioli M, Morse HC, Dalla-Favera R (2002). "c-MYC activates protein kinase A (PKA) by direct transcriptional activation of the PKA catalytic subunit beta (PKA-Cbeta) gene". Oncogene. 21 (51): 7872–82. doi:10.1038/sj.onc.1205986. PMID 12420224.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Higuchi H, Yamashita T, Yoshikawa H, Tohyama M (2003). "PKA phosphorylates the p75 receptor and regulates its localization to lipid rafts". EMBO J. 22 (8): 1790–800. doi:10.1093/emboj/cdg177. PMC 154469. PMID 12682012.
  • Gassel M, Breitenlechner CB, Rüger P, et al. (2003). "Mutants of protein kinase A that mimic the ATP-binding site of protein kinase B (AKT)". J. Mol. Biol. 329 (5): 1021–34. doi:10.1016/S0022-2836(03)00518-7. PMID 12798691.
  • v
  • t
  • e
  • 1apm: 2.0 ANGSTROM REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH A PEPTIDE INHIBITOR AND DETERGENT
    1apm: 2.0 ANGSTROM REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH A PEPTIDE INHIBITOR AND DETERGENT
  • 1atp: 2.2 angstrom refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MNATP and a peptide inhibitor
    1atp: 2.2 angstrom refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MNATP and a peptide inhibitor
  • 1bkx: A BINARY COMPLEX OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE AND ADENOSINE FURTHER DEFINES CONFORMATIONAL FLEXIBILITY
    1bkx: A BINARY COMPLEX OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE AND ADENOSINE FURTHER DEFINES CONFORMATIONAL FLEXIBILITY
  • 1bx6: CRYSTAL STRUCTURE OF THE POTENT NATURAL PRODUCT INHIBITOR BALANOL IN COMPLEX WITH THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE
    1bx6: CRYSTAL STRUCTURE OF THE POTENT NATURAL PRODUCT INHIBITOR BALANOL IN COMPLEX WITH THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE
  • 1cdk: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT (E.C.2.7.1.37) (PROTEIN KINASE A) COMPLEXED WITH PROTEIN KINASE INHIBITOR PEPTIDE FRAGMENT 5-24 (PKI(5-24) ISOELECTRIC VARIANT CA) AND MN2+ ADENYLYL IMIDODIPHOSPHATE (MNAMP-PNP) AT PH 5.6 AND 7C AND 4C
    1cdk: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT (E.C.2.7.1.37) (PROTEIN KINASE A) COMPLEXED WITH PROTEIN KINASE INHIBITOR PEPTIDE FRAGMENT 5-24 (PKI(5-24) ISOELECTRIC VARIANT CA) AND MN2+ ADENYLYL IMIDODIPHOSPHATE (MNAMP-PNP) AT PH 5.6 AND 7C AND 4C
  • 1cmk: CRYSTAL STRUCTURES OF THE MYRISTYLATED CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE REVEAL OPEN AND CLOSED CONFORMATIONS
    1cmk: CRYSTAL STRUCTURES OF THE MYRISTYLATED CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE REVEAL OPEN AND CLOSED CONFORMATIONS
  • 1ctp: STRUCTURE OF THE MAMMALIAN CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE AND AN INHIBITOR PEPTIDE DISPLAYS AN OPEN CONFORMATION
    1ctp: STRUCTURE OF THE MAMMALIAN CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE AND AN INHIBITOR PEPTIDE DISPLAYS AN OPEN CONFORMATION
  • 1fmo: CRYSTAL STRUCTURE OF A POLYHISTIDINE-TAGGED RECOMBINANT CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH THE PEPTIDE INHIBITOR PKI(5-24) AND ADENOSINE
    1fmo: CRYSTAL STRUCTURE OF A POLYHISTIDINE-TAGGED RECOMBINANT CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH THE PEPTIDE INHIBITOR PKI(5-24) AND ADENOSINE
  • 1j3h: Crystal structure of apoenzyme cAMP-dependent protein kinase catalytic subunit
    1j3h: Crystal structure of apoenzyme cAMP-dependent protein kinase catalytic subunit
  • 1jbp: Crystal Structure of the Catalytic Subunit of cAMP-dependent Protein Kinase Complexed with a Substrate Peptide, ADP and Detergent
    1jbp: Crystal Structure of the Catalytic Subunit of cAMP-dependent Protein Kinase Complexed with a Substrate Peptide, ADP and Detergent
  • 1jlu: Crystal Structure of the Catalytic Subunit of cAMP-dependent Protein Kinase Complexed with a Phosphorylated Substrate Peptide and Detergent
    1jlu: Crystal Structure of the Catalytic Subunit of cAMP-dependent Protein Kinase Complexed with a Phosphorylated Substrate Peptide and Detergent
  • 1l3r: Crystal Structure of a Transition State Mimic of the Catalytic Subunit of cAMP-dependent Protein Kinase
    1l3r: Crystal Structure of a Transition State Mimic of the Catalytic Subunit of cAMP-dependent Protein Kinase
  • 1q24: PKA double mutant model of PKB in complex with MgATP
    1q24: PKA double mutant model of PKB in complex with MgATP
  • 1q61: PKA triple mutant model of PKB
    1q61: PKA triple mutant model of PKB
  • 1q62: PKA double mutant model of PKB
    1q62: PKA double mutant model of PKB
  • 1q8t: The Catalytic Subunit of cAMP-dependent Protein Kinase (PKA) in Complex with Rho-kinase Inhibitor Y-27632
    1q8t: The Catalytic Subunit of cAMP-dependent Protein Kinase (PKA) in Complex with Rho-kinase Inhibitor Y-27632
  • 1q8u: The Catalytic Subunit of cAMP-dependent Protein Kinase in Complex with Rho-kinase Inhibitor H-1152P
    1q8u: The Catalytic Subunit of cAMP-dependent Protein Kinase in Complex with Rho-kinase Inhibitor H-1152P
  • 1q8w: The Catalytic Subunit of cAMP-dependent Protein Kinase in Complex with Rho-kinase Inhibitor Fasudil (HA-1077)
    1q8w: The Catalytic Subunit of cAMP-dependent Protein Kinase in Complex with Rho-kinase Inhibitor Fasudil (HA-1077)
  • 1rdq: Hydrolysis of ATP in the crystal of Y204A mutant of cAMP-dependent protein kinase
    1rdq: Hydrolysis of ATP in the crystal of Y204A mutant of cAMP-dependent protein kinase
  • 1re8: Crystal structure of cAMP-dependent protein kinase complexed with balanol analog 2
    1re8: Crystal structure of cAMP-dependent protein kinase complexed with balanol analog 2
  • 1rej: Crystal structure of cAMP-dependent protein kinase complexed with balanol analog 1
    1rej: Crystal structure of cAMP-dependent protein kinase complexed with balanol analog 1
  • 1rek: Crystal structure of cAMP-dependent protein kinase complexed with balanol analog 8
    1rek: Crystal structure of cAMP-dependent protein kinase complexed with balanol analog 8
  • 1smh: Protein kinase A variant complex with completely ordered N-terminal helix
    1smh: Protein kinase A variant complex with completely ordered N-terminal helix
  • 1stc: CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT IN COMPLEX WITH STAUROSPORINE
    1stc: CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT IN COMPLEX WITH STAUROSPORINE
  • 1sve: Crystal Structure of Protein Kinase A in Complex with Azepane Derivative 1
    1sve: Crystal Structure of Protein Kinase A in Complex with Azepane Derivative 1
  • 1svg: Crystal Structure of Protein Kinase A in Complex with Azepane Derivative 4
    1svg: Crystal Structure of Protein Kinase A in Complex with Azepane Derivative 4
  • 1svh: Crystal Structure of Protein Kinase A in Complex with Azepane Derivative 8
    1svh: Crystal Structure of Protein Kinase A in Complex with Azepane Derivative 8
  • 1syk: Crystal structure of E230Q mutant of cAMP-dependent protein kinase reveals unexpected apoenzyme conformation
    1syk: Crystal structure of E230Q mutant of cAMP-dependent protein kinase reveals unexpected apoenzyme conformation
  • 1szm: DUAL BINDING MODE OF BISINDOLYLMALEIMIDE 2 TO PROTEIN KINASE A (PKA)
    1szm: DUAL BINDING MODE OF BISINDOLYLMALEIMIDE 2 TO PROTEIN KINASE A (PKA)
  • 1veb: Crystal Structure of Protein Kinase A in Complex with Azepane Derivative 5
    1veb: Crystal Structure of Protein Kinase A in Complex with Azepane Derivative 5
  • 1xh4: Crystal Structures of Protein Kinase B Selective Inhibitors in Complex with Protein Kinase A and Mutants
    1xh4: Crystal Structures of Protein Kinase B Selective Inhibitors in Complex with Protein Kinase A and Mutants
  • 1xh5: Crystal Structures of Protein Kinase B Selective Inhibitors in Complex with Protein Kinase A and Mutants
    1xh5: Crystal Structures of Protein Kinase B Selective Inhibitors in Complex with Protein Kinase A and Mutants
  • 1xh6: Crystal Structures of Protein Kinase B Selective Inhibitors in Complex with Protein Kinase A and Mutants
    1xh6: Crystal Structures of Protein Kinase B Selective Inhibitors in Complex with Protein Kinase A and Mutants
  • 1xh7: Crystal Structures of Protein Kinase B Selective Inhibitors in Complex with Protein Kinase A and Mutants
    1xh7: Crystal Structures of Protein Kinase B Selective Inhibitors in Complex with Protein Kinase A and Mutants
  • 1xh8: Crystal Structures of Protein Kinase B Selective Inhibitors in Complex with Protein Kinase A and Mutants
    1xh8: Crystal Structures of Protein Kinase B Selective Inhibitors in Complex with Protein Kinase A and Mutants
  • 1xh9: Crystal Structures of Protein Kinase B Selective Inhibitors in Complex with Protein Kinase A and Mutants
    1xh9: Crystal Structures of Protein Kinase B Selective Inhibitors in Complex with Protein Kinase A and Mutants
  • 1xha: Crystal Structures of Protein Kinase B Selective Inhibitors in Complex with Protein Kinase A and Mutants
    1xha: Crystal Structures of Protein Kinase B Selective Inhibitors in Complex with Protein Kinase A and Mutants
  • 1ydr: STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT IN COMPLEX WITH H7 PROTEIN KINASE INHIBITOR 1-(5-ISOQUINOLINESULFONYL)-2-METHYLPIPERAZINE
    1ydr: STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT IN COMPLEX WITH H7 PROTEIN KINASE INHIBITOR 1-(5-ISOQUINOLINESULFONYL)-2-METHYLPIPERAZINE
  • 1yds: STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT IN COMPLEX WITH H8 PROTEIN KINASE INHIBITOR [N-(2-METHYLAMINO)ETHYL]-5-ISOQUINOLINESULFONAMIDE
    1yds: STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT IN COMPLEX WITH H8 PROTEIN KINASE INHIBITOR [N-(2-METHYLAMINO)ETHYL]-5-ISOQUINOLINESULFONAMIDE
  • 1ydt: STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT IN COMPLEX WITH H89 PROTEIN KINASE INHIBITOR N-[2-(4-BROMOCINNAMYLAMINO)ETHYL]-5-ISOQUINOLINE
    1ydt: STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT IN COMPLEX WITH H89 PROTEIN KINASE INHIBITOR N-[2-(4-BROMOCINNAMYLAMINO)ETHYL]-5-ISOQUINOLINE
  • 2c1a: STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-CHLOROBENZYLOXY) ETHYLAMINO)ETHYL)AMIDE
    2c1a: STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-CHLOROBENZYLOXY) ETHYLAMINO)ETHYL)AMIDE
  • 2c1b: STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH (4R,2S)-5'-(4-(4-CHLOROBENZYLOXY)PYRROLIDIN-2-YLMETHANESULFONYL)ISOQUINOLINE
    2c1b: STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH (4R,2S)-5'-(4-(4-CHLOROBENZYLOXY)PYRROLIDIN-2-YLMETHANESULFONYL)ISOQUINOLINE
  • 2cpk: CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CYCLIC ADENOSINE MONOPHOSPHATE-DEPENDENT PROTEIN KINASE
    2cpk: CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CYCLIC ADENOSINE MONOPHOSPHATE-DEPENDENT PROTEIN KINASE
  • 2erz: Crystal Structure of c-AMP Dependent Kinase (PKA) bound to hydroxyfasudil
    2erz: Crystal Structure of c-AMP Dependent Kinase (PKA) bound to hydroxyfasudil
  • 2f7e: PKA complexed with (S)-2-(1H-Indol-3-yl)-1-(5-isoquinolin-6-yl-pyridin-3-yloxymethyl-etylamine
    2f7e: PKA complexed with (S)-2-(1H-Indol-3-yl)-1-(5-isoquinolin-6-yl-pyridin-3-yloxymethyl-etylamine
  • 2f7x: Protein Kinase A bound to (S)-2-(1H-Indol-3-yl)-1-[5-((E)-2-pyridin-4-yl-vinyl)-pyridin-3-yloxymethyl]-ethylamine
    2f7x: Protein Kinase A bound to (S)-2-(1H-Indol-3-yl)-1-[5-((E)-2-pyridin-4-yl-vinyl)-pyridin-3-yloxymethyl]-ethylamine
  • 2f7z: Protein Kinase A bound to (R)-1-(1H-Indol-3-ylmethyl)-2-(2-pyridin-4-yl-[1,7]naphtyridin-5-yloxy)-ehylamine
    2f7z: Protein Kinase A bound to (R)-1-(1H-Indol-3-ylmethyl)-2-(2-pyridin-4-yl-[1,7]naphtyridin-5-yloxy)-ehylamine
  • 2gfc: cAMP-dependent protein kinase PKA catalytic subunit with PKI-5-24
    2gfc: cAMP-dependent protein kinase PKA catalytic subunit with PKI-5-24
  • 2gnf: Protein kinase A fivefold mutant model of Rho-kinase with Y-27632
    2gnf: Protein kinase A fivefold mutant model of Rho-kinase with Y-27632
  • 2gng: Protein kinase A fivefold mutant model of Rho-kinase
    2gng: Protein kinase A fivefold mutant model of Rho-kinase
  • 2gnh: PKA five fold mutant model of Rho-kinase with H1152P
    2gnh: PKA five fold mutant model of Rho-kinase with H1152P
  • 2gni: PKA fivefold mutant model of Rho-kinase with inhibitor Fasudil (HA1077)
    2gni: PKA fivefold mutant model of Rho-kinase with inhibitor Fasudil (HA1077)
  • 2gnj: PKA three fold mutant model of Rho-kinase with Y-27632
    2gnj: PKA three fold mutant model of Rho-kinase with Y-27632
  • 2gnl: PKA threefold mutant model of Rho-kinase with inhibitor H-1152P
    2gnl: PKA threefold mutant model of Rho-kinase with inhibitor H-1152P
  • 2gu8: Discovery of 2-Pyrimidyl-5-Amidothiophenes as Novel and Potent Inhibitors for AKT: Synthesis and SAR Studies
    2gu8: Discovery of 2-Pyrimidyl-5-Amidothiophenes as Novel and Potent Inhibitors for AKT: Synthesis and SAR Studies
  • 2jds: STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH A-443654
    2jds: STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH A-443654
  • 2jdt: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-CHLOROBENZYLOXY) ETHYLAMINO)ETHYL) AMIDE
    2jdt: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-CHLOROBENZYLOXY) ETHYLAMINO)ETHYL) AMIDE
  • 2jdv: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH A-443654
    2jdv: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH A-443654
  • 2oh0: Crystal structure of Protein Kinase A in complex with Pyridine-Pyrazolopyridine Based Inhibitors
    2oh0: Crystal structure of Protein Kinase A in complex with Pyridine-Pyrazolopyridine Based Inhibitors
  • 2ojf: Crystal structure of Protein Kinase A in complex with Pyridine-Pyrazolopyridine based inhibitors
    2ojf: Crystal structure of Protein Kinase A in complex with Pyridine-Pyrazolopyridine based inhibitors
  • 2uvx: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH 7-AZAINDOLE
    2uvx: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH 7-AZAINDOLE
  • 2uvy: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH METHYL-(4-(9H-PURIN-6-YL)-BENZYL)-AMINE
    2uvy: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH METHYL-(4-(9H-PURIN-6-YL)-BENZYL)-AMINE
  • 2uvz: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH C-PHENYL-C-(4-(9H-PURIN-6-YL)-PHENYL)-METHYLAMINE
    2uvz: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH C-PHENYL-C-(4-(9H-PURIN-6-YL)-PHENYL)-METHYLAMINE
  • 2uw0: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH 6-(4-(4-(4-CHLORO-PHENYL)-PIPERIDIN-4-YL)-PHENYL)-9H-PURINE
    2uw0: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH 6-(4-(4-(4-CHLORO-PHENYL)-PIPERIDIN-4-YL)-PHENYL)-9H-PURINE
  • 2uw3: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH 5-METHYL-4-PHENYL-1H-PYRAZOLE
    2uw3: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH 5-METHYL-4-PHENYL-1H-PYRAZOLE
  • 2uw4: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH 2-(4-(5-METHYL-1H-PYRAZOL-4-YL)-PHENYL)-ETHYLAMINE
    2uw4: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH 2-(4-(5-METHYL-1H-PYRAZOL-4-YL)-PHENYL)-ETHYLAMINE
  • 2uw5: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH (R)-2-(4-CHLORO-PHENYL)-2-(4-1H-PYRAZOL-4-YL)-PHENYL)-ETHYLAMINE
    2uw5: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH (R)-2-(4-CHLORO-PHENYL)-2-(4-1H-PYRAZOL-4-YL)-PHENYL)-ETHYLAMINE
  • 2uw6: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH (S)-2-(4-CHLORO-PHENYL)-2-(4-1H-PYRAZOL-4-YL)-PHENYL)-ETHYLAMINE
    2uw6: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH (S)-2-(4-CHLORO-PHENYL)-2-(4-1H-PYRAZOL-4-YL)-PHENYL)-ETHYLAMINE
  • 2uw7: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH 4-(4-CHLORO-PHENYL)-4-(4-(1H-PYRAZOL-4-YL)-PHENYL)-PIPERIDINE
    2uw7: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH 4-(4-CHLORO-PHENYL)-4-(4-(1H-PYRAZOL-4-YL)-PHENYL)-PIPERIDINE
  • 2uw8: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH 2-(4-CHLORO-PHENYL)-2-PHENYL-ETHYLAMINE
    2uw8: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH 2-(4-CHLORO-PHENYL)-2-PHENYL-ETHYLAMINE
  • 2uzt: PKA STRUCTURES OF AKT, INDAZOLE-PYRIDINE INHIBITORS
    2uzt: PKA STRUCTURES OF AKT, INDAZOLE-PYRIDINE INHIBITORS
  • 2uzu: PKA STRUCTURES OF INDAZOLE-PYRIDINE SERIES OF AKT INHIBITORS
    2uzu: PKA STRUCTURES OF INDAZOLE-PYRIDINE SERIES OF AKT INHIBITORS
  • 2uzv: PKA STRUCTURES OF INDAZOLE-PYRIDINE SERIES OF AKT INHIBITORS
    2uzv: PKA STRUCTURES OF INDAZOLE-PYRIDINE SERIES OF AKT INHIBITORS
  • 2uzw: PKA STRUCTURES OF INDAZOLE-PYRIDINE SERIES OF AKT INHIBITORS
    2uzw: PKA STRUCTURES OF INDAZOLE-PYRIDINE SERIES OF AKT INHIBITORS
  • v
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Non-specific serine/threonine protein kinases (EC 2.7.11.1)
Pyruvate dehydrogenase kinase (EC 2.7.11.2)
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)
Myosin-heavy-chain kinase (EC 2.7.11.7)
Fas-activated serine/threonine kinase (EC 2.7.11.8)
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)
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IκB kinase (EC 2.7.11.10)
cAMP-dependent protein kinase (EC 2.7.11.11)
cGMP-dependent protein kinase (EC 2.7.11.12)
Protein kinase C (EC 2.7.11.13)
Rhodopsin kinase (EC 2.7.11.14)
Beta adrenergic receptor kinase (EC 2.7.11.15)
G-protein coupled receptor kinases (EC 2.7.11.16)
Ca2+/calmodulin-dependent (EC 2.7.11.17)
Myosin light-chain kinase (EC 2.7.11.18)
Phosphorylase kinase (EC 2.7.11.19)
Elongation factor 2 kinase (EC 2.7.11.20)
Polo kinase (EC 2.7.11.21)
Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)
Polo kinase (EC 2.7.11.21)
Cyclin-dependent kinase (EC 2.7.11.22)
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)
Mitogen-activated protein kinase (EC 2.7.11.24)
MAP3K (EC 2.7.11.25)
Tau-protein kinase (EC 2.7.11.26)
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)
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Tropomyosin kinase (EC 2.7.11.28)
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Low-density-lipoprotein receptor kinase (EC 2.7.11.29)
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Receptor protein serine/threonine kinase (EC 2.7.11.30)
MAP2K
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