KEGG   ENZYME: 2.7.11.12Help
Entry
EC 2.7.11.12                Enzyme                                 

Name
cGMP-dependent protein kinase;
3':5'-cyclic GMP-dependent protein kinase;
cGMP-dependent protein kinase Ibeta;
guanosine 3':5'-cyclic monophosphate-dependent protein kinase;
PKG;
PKG 1alpha;
PKG 1beta;
PKG II;
STK23
Class
Transferases;
Transferring phosphorus-containing groups;
Protein-serine/threonine kinases
BRITE hierarchy
Sysname
ATP:protein phosphotransferase (cGMP-dependent)
Reaction(IUBMB)
ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
protein [CPD:C00017]
Product
ADP [CPD:C00008];
phosphoprotein [CPD:C00562]
Comment
CGMP is required to activate this enzyme. The enzyme occurs as a dimer in higher eukaryotes. The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites. This domain catalyses the phosphorylation by ATP to specific serine or threonine residues in protein substrates [3]. The enzyme also has two allosteric cGMP-binding sites (sites A and B). Binding of cGMP causes a conformational change that is associated with activation of the kinase [4].
History
EC 2.7.11.12 created 2005 (EC 2.7.1.37 part-incorporated 2005)
Orthology
K07376  cGMP-dependent protein kinase 1
K19477  cGMP-dependent protein kinase 2
Genes
HSA: 5592(PRKG1) 5593(PRKG2)
PTR: 461217(PRKG2) 744467(PRKG1)
PPS: 100975252(PRKG1) 100978260(PRKG2)
GGO: 101139285(PRKG2) 101148943(PRKG1)
PON: 100437791(PRKG1) 100438589(PRKG2)
NLE: 100584834(PRKG2) 100597697(PRKG1)
MCC: 696308(PRKG2) 703356(PRKG1)
MCF: 102122483(PRKG1) 102142098(PRKG2)
CSAB: 103216192(PRKG1) 103235875(PRKG2)
RRO: 104654813(PRKG2) 104676729(PRKG1)
CJC: 100384937(PRKG2) 100388016(PRKG1)
SBQ: 101033123(PRKG2) 101043597(PRKG1)
MMU: 19091(Prkg1) 19092(Prkg2)
RNO: 25523(Prkg2) 54286(Prkg1)
CGE: 100765312(Prkg2) 100768615(Prkg1)
NGI: 103732508(Prkg1) 103735969(Prkg2)
HGL: 101697843(Prkg2) 101708361(Prkg1)
CCAN: 109700389(Prkg1) 109702659(Prkg2)
OCU: 100008694(PRKG1) 100008781(PRKG2)
TUP: 102471472 102489899(PRKG2) 102497341(PRKG1)
CFA: 100855930(PRKG2) 609616(PRKG1)
AML: 100467892(PRKG2) 100481505
UMR: 103661993(PRKG1) 103665352(PRKG2)
FCA: 101091618(PRKG2) 101097420(PRKG1)
PTG: 102949245(PRKG2) 102969150(PRKG1)
AJU: 106969513 106976911(PRKG2)
BTA: 282004(PRKG1) 533330(PRKG2)
BOM: 102269763(PRKG2) 102270503 102279305(PRKG1)
BIU: 109560622(PRKG2) 109579117(PRKG1)
PHD: 102340254(PRKG2) 102344359(PRKG1)
CHX: 102172135(PRKG2) 102182753(PRKG1)
OAS: 101113758(PRKG2) 443010(PRKG1)
SSC: 100512796(PRKG2) 733640(PRKG1)
CFR: 102509252(PRKG1) 102519263(PRKG2)
CDK: 105085256(PRKG1) 105091814(PRKG2)
BACU: 103012801(PRKG1) 103013933(PRKG2)
LVE: 103071917(PRKG1) 103091057(PRKG2)
OOR: 101279276(PRKG1) 101280012(PRKG2)
ECB: 100060358(PRKG2) 100071872(PRKG1)
EPZ: 103549039(PRKG2) 103556704 103563033(PRKG1)
EAI: 106828068(PRKG2) 106847454(PRKG1)
MYB: 102255009(PRKG1) 102258852(PRKG2)
HAI: 109387521(PRKG1) 109387927(PRKG2)
RSS: 109439911(PRKG2) 109450854(PRKG1)
PALE: 102884723(PRKG1) 102894554(PRKG2)
LAV: 100657163(PRKG2) 100662471(PRKG1)
MDO: 100014568(PRKG2) 100023016(PRKG1)
SHR: 100927283(PRKG2) 100928746(PRKG1)
OAA: 100073431(PRKG1) 100075531(PRKG2) 100082499
GGA: 423682(PRKG1) 428753(PRKG2)
MGP: 100540173(PRKG1) 100541294(PRKG2)
CJO: 107312321 107313465(PRKG2) 107315639(PRKG1)
APLA: 101790644(PRKG2) 101802614(PRKG1)
ACYG: 106030263(PRKG1) 106041906(PRKG2)
GFR: 102041315(PRKG1) 102042278(PRKG2)
FAB: 101813345(PRKG2) 101816835(PRKG1)
PHI: 102105641(PRKG1) 102108417(PRKG2)
PMAJ: 107203574(PRKG2) 107207071(PRKG1)
CCW: 104695105(PRKG1) 104697218(PRKG2)
FPG: 101914750(PRKG1) 101916682 101918759(PRKG2)
FCH: 102051167(PRKG1) 102055004(PRKG2) 106631485
CLV: 102089346(PRKG2) 102098659(PRKG1)
EGZ: 104125151(PRKG1) 104133983(PRKG2)
AAM: 106483994 106486427(PRKG1) 106491038(PRKG2)
ASN: 102372581 102375122(PRKG2) 102385836(PRKG1)
AMJ: 102560332(PRKACA) 102570800(PRKG2) 102573015(PRKG1)
PSS: 102462425(PRKG1) 102463494
CMY: 102942713(PRKG1)
CPIC: 101936799 101953224(PRKG1) 103305918(PRKG2)
GJA: 107113865(PRKG1) 107114871(PRKG2)
XLA: 108696071 108696263 108697216 108697357(prkg1.S) 444025(prkg2.L)
XTR: 100494278(prkg1) 100497736(prkg2) 100498055
DRE: 100125912(prkg2) 326020(si:dkey-121j17.5) 394005(prkg1a) 556339
CIN: 100184124
SPU: 585077
DME: Dmel_CG10033(for) Dmel_CG3324(Pkg21D) Dmel_CG4839(CG4839)
DSI: Dsimw501_GD22740(Dsim_GD22740) Dsimw501_GD22942(Dsim_GD22942) Dsimw501_GD23660(Dsim_GD23660)
AME: 406092(For) 551714
NVI: 100114234 100117965(NV50043) 100119839(for)
BMOR: 101735910 692605(PKG-I)
CEL: CELE_F55A8.2(egl-4)
CBR: CBG08401(Cbr-egl-4)
BMY: Bm1_37920
TSP: Tsp_02535
HMG: 100199173 100201371(prkg1)
AQU: 100636239
BOE: 106320190
TCC: 18588547
NTA: 107817514
OEU: 111407855
DCT: 110104152
PPP: 112291101
APRO: F751_6750
PYO: PY17X_1009800(PY02304)
PCB: PCHAS_100910(PC000298.03.0)
TAN: TA04955
TPV: TP03_0511
BBO: BBOV_I004690(19.m02237)
CPV: cgd8_750
TGO: TGME49_311360(PKG)
SMIN: v1.2.000817.t1(symbB.v1.2.000817.t1) v1.2.000877.t1(symbB.v1.2.000877.t1) v1.2.003252.t1(symbB.v1.2.003252.t1) v1.2.004287.t1(symbB.v1.2.004287.t1) v1.2.006098.t1(symbB.v1.2.006098.t1) v1.2.008273.t1(symbB.v1.2.008273.t1) v1.2.008273.t2(symbB.v1.2.008273.t2) v1.2.009118.t1(symbB.v1.2.009118.t1) v1.2.009164.t1(symbB.v1.2.009164.t1) v1.2.010262.t1(symbB.v1.2.010262.t1) v1.2.010262.t2(symbB.v1.2.010262.t2) v1.2.010402.t1(symbB.v1.2.010402.t1) v1.2.011180.t1(symbB.v1.2.011180.t1) v1.2.012476.t1(symbB.v1.2.012476.t1) v1.2.012476.t2(symbB.v1.2.012476.t2) v1.2.015884.t1(symbB.v1.2.015884.t1) v1.2.016972.t2(symbB.v1.2.016972.t2) v1.2.017815.t1(symbB.v1.2.017815.t1) v1.2.022723.t1(symbB.v1.2.022723.t1) v1.2.023087.t1(symbB.v1.2.023087.t1) v1.2.023463.t1(symbB.v1.2.023463.t1) v1.2.023465.t1(symbB.v1.2.023465.t1) v1.2.023864.t1(symbB.v1.2.023864.t1) v1.2.027542.t1(symbB.v1.2.027542.t1) v1.2.031517.t1(symbB.v1.2.031517.t1) v1.2.031929.t1(symbB.v1.2.031929.t1) v1.2.031973.t1(symbB.v1.2.031973.t1) v1.2.033790.t1(symbB.v1.2.033790.t1)
 » show all
Taxonomy
Reference
1  [PMID:186778]
  Authors
Gill GN, Holdy KE, Walton GM, Kanstein CB.
  Title
Purification and characterization of 3':5'-cyclic GMP-dependent protein kinase.
  Journal
Proc Natl Acad Sci U S A 73:3918-22 (1976)
DOI:10.1073/pnas.73.11.3918
Reference
2  [PMID:15312978]
  Authors
Murthy KS.
  Title
Modulation of soluble guanylate cyclase activity by phosphorylation.
  Journal
Neurochem Int 45:845-51 (2004)
DOI:10.1016/j.neuint.2004.03.014
Reference
3  [PMID:12933804]
  Authors
Richie-Jannetta R, Francis SH, Corbin JD.
  Title
Dimerization of cGMP-dependent protein kinase Ibeta is mediated by an extensive amino-terminal leucine zipper motif, and dimerization modulates enzyme function.
  Journal
J Biol Chem 278:50070-9 (2003)
DOI:10.1074/jbc.M306796200
Reference
4  [PMID:9395542]
  Authors
Zhao J, Trewhella J, Corbin J, Francis S, Mitchell R, Brushia R, Walsh D.
  Title
Progressive cyclic nucleotide-induced conformational changes in the cGMP-dependent protein kinase studied by small angle X-ray scattering in solution.
  Journal
J Biol Chem 272:31929-36 (1997)
DOI:10.1074/jbc.272.50.31929
Other DBs
ExplorEnz - The Enzyme Database: 2.7.11.12
IUBMB Enzyme Nomenclature: 2.7.11.12
ExPASy - ENZYME nomenclature database: 2.7.11.12
BRENDA, the Enzyme Database: 2.7.11.12
CAS: 141588-27-4

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