PRKG1

Protein-coding gene in the species Homo sapiens

PRKG1

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
1ZXA, 3OCP, 3OD0, 3OGJ, 4KU7, 4KU8, 4QX5, 4QXK, 4R4L, 4R4M, 4Z07

Identifiers

Aliases

PRKG1, AAT8, PKG, PRKG1B, PRKGR1B, cGK, cGK 1, cGK1, cGKI, cGKI-BETA, cGKI-alpha, protein kinase, cGMP-dependent, type I, PKG1, protein kinase cGMP-dependent 1

External IDs

OMIM: 176894 MGI: 108174 HomoloGene: 55964 GeneCards: PRKG1

Gene location (Human)

Chr.	Chromosome 10 (human)^[1]

Band	10q11.23-q21.1	Start	50,990,888 bp^[1]
Band	10q11.23-q21.1	End	52,298,423 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 19 (mouse)^[2]

Band	19\|19 C1	Start	30,541,889 bp^[2]
Band	19\|19 C1	End	31,742,433 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

saphenous vein

biceps brachii

ascending aorta

right coronary artery

popliteal artery

urethra

superficial temporal artery

right ventricle

left coronary artery

vena cava

Top expressed in

spermatid

trigeminal ganglion

soleus muscle

sternocleidomastoid muscle

digastric muscle

temporal muscle

intercostal muscle

semi-lunar valve

triceps brachii muscle

ciliary body

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	transferase activity nucleotide binding calcium channel regulator activity cGMP binding kinase activity protein binding catalytic activity ATP binding protein serine/threonine kinase activity cGMP-dependent protein kinase activity identical protein binding protein kinase activity
Cellular component	cytoplasm cytosol Golgi apparatus plasma membrane
Biological process	negative regulation of smooth muscle contraction phosphorylation regulation of GTPase activity dendrite development neuron migration negative regulation of platelet aggregation cGMP-mediated signaling relaxation of vascular associated smooth muscle forebrain development metabolism actin cytoskeleton organization signal transduction protein phosphorylation negative regulation of vascular associated smooth muscle cell proliferation negative regulation of vascular associated smooth muscle cell migration
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


5592


19091

Ensembl


ENSG00000185532


ENSMUSG00000052920

UniProt


Q13976


P0C605

RefSeq (mRNA)


NM_001098512 NM_006258 NM_001374781 NM_001374782


NM_001013833 NM_011160

RefSeq (protein)


NP_001091982 NP_006249 NP_001361710 NP_001361711


NP_001013855 NP_035290

Location (UCSC)

Chr 10: 50.99 – 52.3 Mb

Chr 19: 30.54 – 31.74 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

cGMP-dependent protein kinase 1, alpha isozyme is an enzyme that in humans is encoded by the PRKG1 gene.^[5]^[6]^[7]

Interactions

PRKG1 has been shown to interact with:

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000185532 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000052920 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Sandberg M, Natarajan V, Ronander I, Kalderon D, Walter U, Lohmann SM, Jahnsen T (Sep 1989). "Molecular cloning and predicted full-length amino acid sequence of the type I beta isozyme of cGMP-dependent protein kinase from human placenta. Tissue distribution and developmental changes in rat". FEBS Letters. 255 (2): 321–9. doi:10.1016/0014-5793(89)81114-7. PMID 2792381. S2CID 83233954.
^ Orstavik S, Sandberg M, Bérubé D, Natarajan V, Simard J, Walter U, Gagné R, Hansson V, Jahnsen T (April 1992). "Localization of the human gene for the type I cyclic GMP-dependent protein kinase to chromosome 10". Cytogenetics and Cell Genetics. 59 (4): 270–3. doi:10.1159/000133267. PMID 1544322.
^ "Entrez Gene: PRKG1 protein kinase, cGMP-dependent, type I".
^ Casteel DE, Zhuang S, Gudi T, Tang J, Vuica M, Desiderio S, Pilz RB (Aug 2002). "cGMP-dependent protein kinase I beta physically and functionally interacts with the transcriptional regulator TFII-I". The Journal of Biological Chemistry. 277 (35): 32003–14. doi:10.1074/jbc.M112332200. PMID 12082086.
^ ^a ^b Schlossmann J, Ammendola A, Ashman K, Zong X, Huber A, Neubauer G, Wang GX, Allescher HD, Korth M, Wilm M, Hofmann F, Ruth P (Mar 2000). "Regulation of intracellular calcium by a signalling complex of IRAG, IP3 receptor and cGMP kinase Ibeta". Nature. 404 (6774): 197–201. Bibcode:2000Natur.404..197S. doi:10.1038/35004606. PMID 10724174. S2CID 205004996.
^ Ammendola A, Geiselhöringer A, Hofmann F, Schlossmann J (Jun 2001). "Molecular determinants of the interaction between the inositol 1,4,5-trisphosphate receptor-associated cGMP kinase substrate (IRAG) and cGMP kinase Ibeta". The Journal of Biological Chemistry. 276 (26): 24153–9. doi:10.1074/jbc.M101530200. PMID 11309393.
^ Tang KM, Wang GR, Lu P, Karas RH, Aronovitz M, Heximer SP, Kaltenbronn KM, Blumer KJ, Siderovski DP, Zhu Y, Mendelsohn ME, Tang M, Wang G (Dec 2003). "Regulator of G-protein signaling-2 mediates vascular smooth muscle relaxation and blood pressure". Nature Medicine. 9 (12): 1506–12. doi:10.1038/nm958. PMID 14608379. S2CID 20331752.
^ Yuasa K, Michibata H, Omori K, Yanaka N (Dec 1999). "A novel interaction of cGMP-dependent protein kinase I with troponin T". The Journal of Biological Chemistry. 274 (52): 37429–34. doi:10.1074/jbc.274.52.37429. PMID 10601315.

Picciotto MR, Cohn JA, Bertuzzi G, Greengard P, Nairn AC (Jun 1992). "Phosphorylation of the cystic fibrosis transmembrane conductance regulator". The Journal of Biological Chemistry. 267 (18): 12742–52. doi:10.1016/S0021-9258(18)42339-3. PMID 1377674.
Thomas MK, Francis SH, Corbin JD (Sep 1990). "Substrate- and kinase-directed regulation of phosphorylation of a cGMP-binding phosphodiesterase by cGMP". The Journal of Biological Chemistry. 265 (25): 14971–8. doi:10.1016/S0021-9258(18)77211-6. PMID 2168396.
Pöhler D, Butt E, Meissner J, Müller S, Lohse M, Walter U, Lohmann SM, Jarchau T (Nov 1995). "Expression, purification, and characterization of the cGMP-dependent protein kinases I beta and II using the baculovirus system". FEBS Letters. 374 (3): 419–25. doi:10.1016/0014-5793(95)01168-E. PMID 7589584. S2CID 25634004.
Komalavilas P, Lincoln TM (Mar 1994). "Phosphorylation of the inositol 1,4,5-trisphosphate receptor by cyclic GMP-dependent protein kinase". The Journal of Biological Chemistry. 269 (12): 8701–7. doi:10.1016/S0021-9258(17)37024-2. PMID 8132598.
Butt E, Abel K, Krieger M, Palm D, Hoppe V, Hoppe J, Walter U (May 1994). "cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets". The Journal of Biological Chemistry. 269 (20): 14509–17. doi:10.1016/S0021-9258(17)36652-8. PMID 8182057.
Suko J, Maurer-Fogy I, Plank B, Bertel O, Wyskovsky W, Hohenegger M, Hellmann G (Jan 1993). "Phosphorylation of serine 2843 in ryanodine receptor-calcium release channel of skeletal muscle by cAMP-, cGMP- and CaM-dependent protein kinase". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1175 (2): 193–206. doi:10.1016/0167-4889(93)90023-I. PMID 8380342.
Tamura N, Itoh H, Ogawa Y, Nakagawa O, Harada M, Chun TH, Suga S, Yoshimasa T, Nakao K (Mar 1996). "cDNA cloning and gene expression of human type Ialpha cGMP-dependent protein kinase". Hypertension. 27 (3 Pt 2): 552–7. doi:10.1161/01.hyp.27.3.552. PMID 8613202.
Salih E, Zhou HY, Glimcher MJ (Jul 1996). "Phosphorylation of purified bovine bone sialoprotein and osteopontin by protein kinases". The Journal of Biological Chemistry. 271 (28): 16897–905. doi:10.1074/jbc.271.28.16897. PMID 8663267.
Xing J, Ginty DD, Greenberg ME (Aug 1996). "Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase". Science. 273 (5277): 959–63. Bibcode:1996Sci...273..959X. doi:10.1126/science.273.5277.959. PMID 8688081. S2CID 22226803.
Orstavik S, Natarajan V, Taskén K, Jahnsen T, Sandberg M (Jun 1997). "Characterization of the human gene encoding the type I alpha and type I beta cGMP-dependent protein kinase (PRKG1)". Genomics. 42 (2): 311–8. doi:10.1006/geno.1997.4743. PMID 9192852.
Deak M, Clifton AD, Lucocq LM, Alessi DR (Aug 1998). "Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB". The EMBO Journal. 17 (15): 4426–41. doi:10.1093/emboj/17.15.4426. PMC 1170775. PMID 9687510.
Du K, Montminy M (Dec 1998). "CREB is a regulatory target for the protein kinase Akt/PKB". The Journal of Biological Chemistry. 273 (49): 32377–9. doi:10.1074/jbc.273.49.32377. PMID 9829964.
Endo S, Suzuki M, Sumi M, Nairn AC, Morita R, Yamakawa K, Greengard P, Ito M (Mar 1999). "Molecular identification of human G-substrate, a possible downstream component of the cGMP-dependent protein kinase cascade in cerebellar Purkinje cells". Proceedings of the National Academy of Sciences of the United States of America. 96 (5): 2467–72. Bibcode:1999PNAS...96.2467E. doi:10.1073/pnas.96.5.2467. PMC 26808. PMID 10051666.
Wang X, Bruderer S, Rafi Z, Xue J, Milburn PJ, Krämer A, Robinson PJ (Aug 1999). "Phosphorylation of splicing factor SF1 on Ser20 by cGMP-dependent protein kinase regulates spliceosome assembly". The EMBO Journal. 18 (16): 4549–59. doi:10.1093/emboj/18.16.4549. PMC 1171529. PMID 10449420.
Surks HK, Mochizuki N, Kasai Y, Georgescu SP, Tang KM, Ito M, Lincoln TM, Mendelsohn ME (Nov 1999). "Regulation of myosin phosphatase by a specific interaction with cGMP- dependent protein kinase Ialpha". Science. 286 (5444): 1583–7. doi:10.1126/science.286.5444.1583. PMID 10567269.
Yuasa K, Michibata H, Omori K, Yanaka N (Dec 1999). "A novel interaction of cGMP-dependent protein kinase I with troponin T". The Journal of Biological Chemistry. 274 (52): 37429–34. doi:10.1074/jbc.274.52.37429. PMID 10601315.
Yuasa K, Omori K, Yanaka N (Feb 2000). "Binding and phosphorylation of a novel male germ cell-specific cGMP-dependent protein kinase-anchoring protein by cGMP-dependent protein kinase Ialpha". The Journal of Biological Chemistry. 275 (7): 4897–905. doi:10.1074/jbc.275.7.4897. PMID 10671526.
Huber A, Neuhuber WL, Klugbauer N, Ruth P, Allescher HD (Feb 2000). "Cysteine-rich protein 2, a novel substrate for cGMP kinase I in enteric neurons and intestinal smooth muscle". The Journal of Biological Chemistry. 275 (8): 5504–11. doi:10.1074/jbc.275.8.5504. PMID 10681529.

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 mTOR EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1
Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3 PDK4
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 Aurora C 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 CAMK1A CAMK1B CAMK1D CAMK1G CAMK2 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

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)