PRKACB

Identifiers

PRKACB, PKA C-beta, PKACB, protein kinase cAMP-activated catalytic subunit beta

External IDs

MGI: 97594 HomoloGene: 121718 GeneCards: PRKACB

Targeted by Drug

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
Cellular component	• cytoplasm • cytosol • centrosome • membrane • plasma membrane • nucleoplasm • ciliary base • perinuclear region of cytoplasm • cAMP-dependent protein kinase complex • extracellular exosome • nucleus
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 • lipoprotein metabolic process
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

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_001164198 NM_001164199 NM_001164200 NM_011100

RefSeq (protein)

NP_001229786.1 NP_001229787.1 NP_001229788.1 NP_001229789.1 NP_001229790.1
NP_001229791.1 NP_001287844.1 NP_001287845.1 NP_001287846.1 NP_002722.1 NP_891993.1 NP_997461.1 NP_002722.1


NP_001157670.1 NP_001157671.1 NP_001157672.1 NP_035230.1

Location (UCSC)

Chr 1: 84.08 – 84.24 Mb

Chr 3: 146.73 – 146.81 Mb

PubMed search

^[2]

^[3]

Wikidata

View/Edit Human

View/Edit Mouse

cAMP-dependent protein kinase catalytic subunit beta is an enzyme that in humans is encoded by the PRKACB gene.^[4]

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 Ser/Thr protein kinase family and is a catalytic subunit of PKA. Three alternatively spliced transcript variants encoding distinct isoforms have been observed.^[4]

Interactions

PRKACB has been shown to interact with Ryanodine receptor 2^[5] and Low affinity nerve growth factor receptor.^[6]

References

↑ "Drugs that physically interact with cAMP-dependent protein kinase catalytic subunit beta view/edit references on wikidata".
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
1 2 "Entrez Gene: PRKACB protein kinase, cAMP-dependent, catalytic, beta".
↑ Marx, S O; 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. UNITED STATES. 101 (4): 365–76. doi:10.1016/S0092-8674(00)80847-8. ISSN 0092-8674. PMID 10830164.
↑ Higuchi, Haruhisa; Yamashita Toshihide; Yoshikawa Hideki; Tohyama Masaya (April 2003). "PKA phosphorylates the p75 receptor and regulates its localization to lipid rafts". EMBO J. England. 22 (8): 1790–800. doi:10.1093/emboj/cdg177. ISSN 0261-4189. PMC 154469. PMID 12682012.

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.
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. 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. 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. 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. 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.
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. 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. 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.

PDB gallery

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

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

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

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

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

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

1q24: PKA double mutant model of PKB in complex with MgATP

1q61: PKA triple 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

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)

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

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

1smh: Protein kinase A variant complex with completely ordered N-terminal helix

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

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

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)

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

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

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

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

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

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

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

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

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

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

2gng: Protein kinase A fivefold mutant model of Rho-kinase

2gnh: PKA five fold mutant model of Rho-kinase with H1152P

2gni: PKA fivefold mutant model of Rho-kinase with inhibitor Fasudil (HA1077)

2gnj: PKA three fold mutant model of Rho-kinase with Y-27632

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

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

2jdv: STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH A-443654

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

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

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

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

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

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

2uzt: PKA STRUCTURES OF AKT, INDAZOLE-PYRIDINE INHIBITORS

2uzu: 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

Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated Mammalian target of rapamycin EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1

Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3

Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3

3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB

(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G

(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4

Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase

Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10

Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-

IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP

cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY

cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1

Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3

Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase

Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2

G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6

Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1

Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4

Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2

Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1

(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1

Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14

MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14

Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3

(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-

Tropomyosin kinase (EC 2.7.11.28)	-

Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-

Receptor protein serine/threonine kinase (EC 2.7.11.30)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

This article is issued from Wikipedia - version of the 5/25/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.

PRKACB

Interactions

References

Further reading