cGMP-dependent protein kinase 1 - Homo sapiens (Human)

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Preferred order of sections

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Protein names

Recommended name:
cGMP-dependent protein kinase 1
Short name=cGK 1
Short name=cGK1
EC=2.7.11.12

Alternative name(s):
cGMP-dependent protein kinase I
Short name=cGKI

Gene names

Name:	PRKG1
Synonyms:	PRKG1B, PRKGR1A, PRKGR1B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Sequence length	671 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

Function	Serine/threonine protein kinase that acts as key mediator of the nitric oxide (NO)/cGMP signaling pathway. GMP binding activates PRKG1, which phosphorylates serines and threonines on many cellular proteins. Numerous protein targets for PRKG1 phosphorylation are implicated in modulating cellular calcium, but the contribution of each of these targets may vary substantially among cell types. Proteins that are phosphorylated by PRKG1 regulate platelet activation and adhesion, smooth muscle contraction, cardiac function, gene expression, feedback of the NO-signaling pathway, and other processes involved in several aspects of the CNS like axon guidance, hippocampal and cerebellar learning, circadian rhythm and nociception. Smooth muscle relaxation is mediated through lowering of intracellular free calcium, by desensitization of contractile proteins to calcium, and by decrease in the contractile state of smooth muscle or in platelet activation. Regulates intracellular calcium levels via several pathways: phosphorylates MRVI1/IRAG and inhibits IP3-induced Ca²⁺ release from intracellular stores, phosphorylation of KCNMA1 (BKCa) channels decreases intracellular Ca²⁺ levels, which leads to increased opening of this channel. PRKG1 phosphorylates the canonical transient receptor potential channel (TRPC) family which inactivates the associated inward calcium current. Another mode of action of NO/cGMP/PKGI signaling involves PKGI-mediated inactivation of the Ras homolog gene family member A (RhoA). Phosphorylation of RHOA by PRKG1 blocks the action of this protein in myriad processes: regulation of RHOA translocation; decreasing contraction; controlling vesicle trafficking, reduction of myosin light chain phosphorylation resulting in vasorelaxation. Activation of PRKG1 by NO signaling alters also gene expression in a number of tissues. In smooth muscle cells, increased cGMP and PRKG1 activity influence expression of smooth muscle-specific contractile proteins, levels of proteins in the NO/cGMP signaling pathway, down-regulation of the matrix proteins osteopontin and thrombospondin-1 to limit smooth muscle cell migration and phenotype. Regulates vasodilator-stimulated phosphoprotein (VASP) functions in platelets and smooth muscle. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.21
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	In the absence of cGMP, PRKG1 activity is suppressed by autoinhibitory contacts.
Subunit structure	Isoform alpha: parallel homodimer or heterodimer and also heterotetramer. Interacts directly with PPP1R12A. Non-covalent dimer of dimer of PRKG1-PRKG1 and PPP1R12A-PPP1R12A. This interaction targets PRKG1 to stress fibers to mediate smooth muscle cell relaxation and vasodilation in responses to rises in cGMP. Isoform beta: antiparallel homodimer. Part of cGMP kinase signaling complex at least composed of ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and ITPR1 By similarity. Interacts with MRVI1. Forms a stable complex with ITPR1, MRVI1, and isoform beta of PRKG1. Interacts with TRPC7 (via ankyrin repeat domain). Isoform alpha interacts with RGS2. Interacts with GTF2I. Ref.9 Ref.11 Ref.13 Ref.15 Ref.16 Ref.17 Ref.21 Ref.22 Ref.23
Subcellular location	Cytoplasm By similarity. Note: Colocalized with TRPC7 in the plasma membrane By similarity. Ref.15 Ref.21
Tissue specificity	Primarily expressed in lung and placenta. Ref.4
Domain	Composed of an N-terminal leucine-zipper domain followed by an autoinhibitory domain, which mediate homodimer formation and inhibit kinase activity, respectively. Next, two cGMP-binding domains are followed by the catalytic domain at the C-terminus. Binding of cGMP to cGMP-binding domains results in a conformational change that activates kinase activity by removing the autoinhibitory domain from the catalytic cleft leaving the catalytic domain free to phosphorylate downstream substrates. Isoforms alpha and beta have identical cGMP-binding and catalytic domains but differ in their leucine zipper and autoinhibitory sequences and therefore differ in their dimerization substrates and kinase enzyme activity. Heterotetramerization is mediated by the interaction between a coiled-coil of PRKG1 and the leucine/isoleucine zipper of PPP1R12A/MBS, the myosin-binding subunit of the myosin phosphatase.
Post-translational modification	Autophosphorylation increases kinase activity. 65 kDa monomer is produced by proteolytic cleavage By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. cGMP subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 2 cyclic nucleotide-binding domains. Contains 1 protein kinase domain.

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding cGMP cGMP-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	3D-structure Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Traceable author statement PubMed 10851246. Source: ProtInc blood coagulation Traceable author statement. Source: Reactome dendrite development Inferred from electronic annotation. Source: Compara forebrain development Inferred from electronic annotation. Source: Compara negative regulation of platelet aggregation Inferred from mutant phenotype Ref.15. Source: UniProtKB neuron migration Inferred from electronic annotation. Source: Compara regulation of GTPase activity Inferred from mutant phenotype Ref.13. Source: UniProtKB signal transduction Traceable author statement Ref.1. Source: ProtInc
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome plasma membrane Inferred from direct assay Ref.21 Ref.15. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cGMP binding Inferred from electronic annotation. Source: UniProtKB-KW cGMP-dependent protein kinase activity Inferred from direct assay Ref.21. Source: UniProtKB calcium channel regulator activity Inferred from direct assay Ref.21. Source: UniProtKB
Complete GO annotation...

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Initiator methionine

1

Removed By similarity

Chain

2 – 671

670

cGMP-dependent protein kinase 1

PRO_0000086115

Domain

360 – 619

260

Protein kinase

Domain

620 – 671

52

AGC-kinase C-terminal

Nucleotide binding

167 – 170

4

cAMP or cGMP

Nucleotide binding

177 – 178

2

cAMP or cGMP

Nucleotide binding

366 – 374

9

ATP By similarity

Region

2 – 102

101

Required for dimerization

Region

9 – 44

36

Leucine-zipper

Region

50 – 75

26

Autoinhibitory domain By similarity

Region

103 – 220

118

cGMP-binding, high affinity

Region

221 – 341

121

cGMP-binding, low affinity

Active site

484

1

Proton acceptor By similarity

Binding site

390

1

ATP By similarity

Modified residue

2

1

N-acetylserine By similarity

Modified residue

59

1

Phosphothreonine; by autocatalysis By similarity

Disulfide bond

43

Interchain By similarity

Alternative sequence

1 – 89

89

MSELE…TKSER → MGTLRDLQYALQEKIEELRQ RDALIDELELELDQKDELIQ KLQNELDKYRSVIRPATQQA QKQSASTLQGEPRTKRQAIS AEPTAFDIQDLSHVTLPFYP KSPQ in isoform Beta.

VSP_038714

Natural variant

249

1

I → V. Ref.25
Corresponds to variant rs56082459 [ dbSNP | Ensembl ].

VAR_046773

Natural variant

267

1

N → S. Ref.25
Corresponds to variant rs34997494 [ dbSNP | Ensembl ].

VAR_051632

Mutagenesis

12

1

L → A: Loss of binding to PPP1R12A. Ref.9

Mutagenesis

19

1

I → A: Loss of binding to PPP1R12A. Ref.9

Mutagenesis

26

1

L → P: Loss of binding to PPP1R12A. Ref.9

Mutagenesis

33

1

I → A: Loss of binding to PPP1R12A. Ref.9

Mutagenesis

40

1

L → A: Loss of binding to PPP1R12A. Ref.9

1

.

671

Helix Strand Turn

Details...

Sequence		Length	Mass (Da)
Isoform Alpha (CGK1-alpha) [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 51389502A5E5FBD2 Show »	FASTA	671	76,364
10 20 30 40 50 60 MSELEEDFAK ILMLKEERIK ELEKRLSEKE EEIQELKRKL HKCQSVLPVP STHIGPRTTR 70 80 90 100 110 120 AQGISAEPQT YRSFHDLRQA FRKFTKSERS KDLIKEAILD NDFMKNLELS QIQEIVDCMY 130 140 150 160 170 180 PVEYGKDSCI IKEGDVGSLV YVMEDGKVEV TKEGVKLCTM GPGKVFGELA ILYNCTRTAT 190 200 210 220 230 240 VKTLVNVKLW AIDRQCFQTI MMRTGLIKHT EYMEFLKSVP TFQSLPEEIL SKLADVLEET 250 260 270 280 290 300 HYENGEYIIR QGARGDTFFI ISKGTVNVTR EDSPSEDPVF LRTLGKGDWF GEKALQGEDV 310 320 330 340 350 360 RTANVIAAEA VTCLVIDRDS FKHLIGGLDD VSNKAYEDAE AKAKYEAEAA FFANLKLSDF 370 380 390 400 410 420 NIIDTLGVGG FGRVELVQLK SEESKTFAMK ILKKRHIVDT RQQEHIRSEK QIMQGAHSDF 430 440 450 460 470 480 IVRLYRTFKD SKYLYMLMEA CLGGELWTIL RDRGSFEDST TRFYTACVVE AFAYLHSKGI 490 500 510 520 530 540 IYRDLKPENL ILDHRGYAKL VDFGFAKKIG FGKKTWTFCG TPEYVAPEII LNKGHDISAD 550 560 570 580 590 600 YWSLGILMYE LLTGSPPFSG PDPMKTYNII LRGIDMIEFP KKIAKNAANL IKKLCRDNPS 610 620 630 640 650 660 ERLGNLKNGV KDIQKHKWFE GFNWEGLRKG TLTPPIIPSV ASPTDTSNFD SFPEDNDEPP 670 PDDNSGWDID F « Hide
Isoform Beta (CGK1-beta) [UniParc] [UniParc]. Checksum: A097041AB284F1E6 Show »	FASTA	686	77,804
10 20 30 40 50 60 MGTLRDLQYA LQEKIEELRQ RDALIDELEL ELDQKDELIQ KLQNELDKYR SVIRPATQQA 70 80 90 100 110 120 QKQSASTLQG EPRTKRQAIS AEPTAFDIQD LSHVTLPFYP KSPQSKDLIK EAILDNDFMK 130 140 150 160 170 180 NLELSQIQEI VDCMYPVEYG KDSCIIKEGD VGSLVYVMED GKVEVTKEGV KLCTMGPGKV 190 200 210 220 230 240 FGELAILYNC TRTATVKTLV NVKLWAIDRQ CFQTIMMRTG LIKHTEYMEF LKSVPTFQSL 250 260 270 280 290 300 PEEILSKLAD VLEETHYENG EYIIRQGARG DTFFIISKGT VNVTREDSPS EDPVFLRTLG 310 320 330 340 350 360 KGDWFGEKAL QGEDVRTANV IAAEAVTCLV IDRDSFKHLI GGLDDVSNKA YEDAEAKAKY 370 380 390 400 410 420 EAEAAFFANL KLSDFNIIDT LGVGGFGRVE LVQLKSEESK TFAMKILKKR HIVDTRQQEH 430 440 450 460 470 480 IRSEKQIMQG AHSDFIVRLY RTFKDSKYLY MLMEACLGGE LWTILRDRGS FEDSTTRFYT 490 500 510 520 530 540 ACVVEAFAYL HSKGIIYRDL KPENLILDHR GYAKLVDFGF AKKIGFGKKT WTFCGTPEYV 550 560 570 580 590 600 APEIILNKGH DISADYWSLG ILMYELLTGS PPFSGPDPMK TYNIILRGID MIEFPKKIAK 610 620 630 640 650 660 NAANLIKKLC RDNPSERLGN LKNGVKDIQK HKWFEGFNWE GLRKGTLTPP IIPSVASPTD 670 680 TSNFDSFPED NDEPPPDDNS GWDIDF « Hide

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Sandberg M., Natarajan V., Ronander I., Kalderon D., Walter U., Lohmann S.M., Jahnsen T. FEBS Lett. 255:321-329(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA). Tissue: Placenta.
[2]	Sandberg M. Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"cDNA cloning and gene expression of human type Ialpha cGMP-dependent protein kinase." Tamura N., Itoh H., Ogawa Y., Nakagawa O., Harada M., Chun T., Suga S., Yoshimasa T., Nakao K. Hypertension 27:552-557(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA). Tissue: Lung.
[4]	"Characterization of the human gene encoding the type I alpha and type I beta cGMP-dependent protein kinase (PRKG1)." Orstavik S., Natarajan V., Tasken K., Jahnsen T., Sandberg M. Genomics 42:311-318(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
[5]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
[8]	"cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets." Butt E., Abel K., Krieger M., Palm D., Hoppe V., Hoppe J., Walter U. J. Biol. Chem. 269:14509-14517(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF VASP.
[9]	"Regulation of myosin phosphatase by a specific interaction with cGMP-dependent protein kinase Ialpha." Surks H.K., Mochizuki N., Kasai Y., Georgescu S.P., Tang K.M., Ito M., Lincoln T.M., Mendelsohn M.E. Science 286:1583-1587(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PPP1R12A, SUBUNIT, MUTAGENESIS OF LEU-12; ILE-19; LEU-26; ILE-33 AND LEU-40, FUNCTION.
[10]	"cGMP-dependent protein kinase phosphorylates and inactivates RhoA." Sawada N., Itoh H., Yamashita J., Doi K., Inoue M., Masatsugu K., Fukunaga Y., Sakaguchi S., Sone M., Yamahara K., Yurugi T., Nakao K. Biochem. Biophys. Res. Commun. 280:798-805(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF RHOA.
[11]	"cGMP-dependent protein kinase I beta physically and functionally interacts with the transcriptional regulator TFII-I." Casteel D.E., Zhuang S., Gudi T., Tang J., Vuica M., Desiderio S., Pilz R.B. J. Biol. Chem. 277:32003-32014(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF GTF2I, INTERACTION WITH GTF2I.
[12]	"Regulation of cGMP-specific phosphodiesterase (PDE5) phosphorylation in smooth muscle cells." Rybalkin S.D., Rybalkina I.G., Feil R., Hofmann F., Beavo J.A. J. Biol. Chem. 277:3310-3317(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PDE5.
[13]	"Regulator of G-protein signaling-2 mediates vascular smooth muscle relaxation and blood pressure." Tang K.M., Wang G.R., Lu P., Karas R.H., Aronovitz M., Heximer S.P., Kaltenbronn K.M., Blumer K.J., Siderovski D.P., Zhu Y., Mendelsohn M.E. Nat. Med. 9:1506-1512(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF RGS2, INTERACTION WITH RGS2.
[14]	"Smooth muscle phosphatase is regulated in vivo by exclusion of phosphorylation of threonine 696 of MYPT1 by phosphorylation of Serine 695 in response to cyclic nucleotides." Wooldridge A.A., MacDonald J.A., Erdodi F., Ma C., Borman M.A., Hartshorne D.J., Haystead T.A.J. J. Biol. Chem. 279:34496-34504(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation and thrombus formation." Antl M., von Bruehl M.-L., Eiglsperger C., Werner M., Konrad I., Kocher T., Wilm M., Hofmann F., Massberg S., Schlossmann J. Blood 109:552-559(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN THE INHIBITION OF PLATELET AGGREGATION, FUNCTION IN PHOSPHORYLATION OF MRVI1, SUBCELLULAR LOCATION, INTERACTION WITH MRVI1 AND ITPR1.
[16]	"Interactions between the leucine-zipper motif of cGMP-dependent protein kinase and the C-terminal region of the targeting subunit of myosin light chain phosphatase." Lee E., Hayes D.B., Langsetmo K., Sundberg E.J., Tao T.C. J. Mol. Biol. 373:1198-1212(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PPP1R12A.
[17]	"Probing the interaction between the coiled coil leucine zipper of cGMP-dependent protein kinase Ialpha and the C terminus of the myosin binding subunit of the myosin light chain phosphatase." Sharma A.K., Zhou G.-P., Kupferman J., Surks H.K., Christensen E.N., Chou J.J., Mendelsohn M.E., Rigby A.C. J. Biol. Chem. 283:32860-32869(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PPP1R12A, SUBUNIT.
[18]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"cGMP-dependent protein kinases and cGMP phosphodiesterases in nitric oxide and cGMP action." Francis S.H., Busch J.L., Corbin J.D., Sibley D. Pharmacol. Rev. 62:525-563(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[20]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"Functional regulation of transient receptor potential canonical 7 by cGMP-dependent protein kinase Ialpha." Yuasa K., Matsuda T., Tsuji A. Cell. Signal. 23:1179-1187(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION (ISOFORM ALPHA) IN PHOSPHORYLATION OF TRPC7, INTERACTION WITH TRPC7, SUBCELLULAR LOCATION.
[22]	"Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: application to cGMP-dependent protein kinase Ialpha." Schnell J.R., Zhou G.-P., Zweckstetter M., Rigby A.C., Chou J.J. Protein Sci. 14:2421-2428(2005) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 2-58, INTERACTION WITH PPP1R12A, SUBUNIT.
[23]	"A crystal structure of the cyclic GMP-dependent protein kinase I{beta} dimerization/docking domain reveals molecular details of isoform-specific anchoring." Casteel D.E., Smith-Nguyen E.V., Sankaran B., Roh S.H., Pilz R.B., Kim C. J. Biol. Chem. 285:32684-32688(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 4-55 (ISOFORM BETA), SUBUNIT.
[24]	"Co-crystal structures of PKG Ibeta (92-227) with cGMP and cAMP reveal the molecular details of cyclic-nucleotide binding." Kim J.J., Casteel D.E., Huang G., Kwon T.H., Ren R.K., Zwart P., Headd J.J., Brown N.G., Chow D.C., Palzkill T., Kim C. PLoS ONE 6:E18413-E18413(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 92-227 (ISOFORM BETA) IN COMPLEX WITH CGMP AND CAMP.
[25]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-249 AND SER-267.
+	Additional computationally mapped references.

EMBL
GenBank
DDBJ

Y07512 mRNA. Translation: CAA68810.1.
D45864 mRNA. Translation: BAA08297.1.
Z92867

Z92885 Genomic DNA. Translation: CAB07436.1.
Z92868

Z92885 Genomic DNA. Translation: CAB07437.1.
AL391378

AC026228 Genomic DNA. Translation: CAI39626.1.
AL928686

AC022025 Genomic DNA. Translation: CAI40743.1.
AL157399

AC022537 Genomic DNA. Translation: CAI41305.1.
AL731537

AC009986 Genomic DNA. Translation: CAI17115.1.
CH471083 Genomic DNA. Translation: EAW54140.1.
BC062688 mRNA. Translation: AAH62688.1.
BC127090 mRNA. Translation: AAI27091.1.

IPI

IPI00427586.
IPI00436355.

PIR

S05702.

RefSeq

NP_001091982.1. NM_001098512.2.
NP_006249.1. NM_006258.3.

UniGene

Hs.407535.

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZXA	NMR	-	A/B	2-58	[»]
3NMD	X-ray	2.27	A/B/C/D/E	4-55	[»]
3OCP	X-ray	2.49	A/B	92-227	[»]
3OD0	X-ray	2.90	A/B	92-227	[»]
3OGJ	X-ray	2.75	A/B/C/D	92-219	[»]

ProteinModelPortal

Q13976.

ModBase

Search...

DIP

DIP-46288N.

MINT

MINT-121708.

STRING

9606.ENSP00000363092.

PhosphoSite

Q13976.

DMDM

6225588.

PaxDb

Q13976.

PRIDE

Q13976.

DNASU

5592.

StructuralBiologyKnowledgebase

Search...

Ensembl

ENST00000373980; ENSP00000363092; ENSG00000185532.
ENST00000401604; ENSP00000384200; ENSG00000185532.

GeneID

5592.

KEGG

hsa:5592.

UCSC

uc001jjm.3. human.
uc001jjo.3. human.

CTD

5592.

GeneCards

GC10P052751.

HGNC

HGNC:9414. PRKG1.

HPA

CAB009629.
HPA007699.

MIM

176894. gene.

neXtProt

NX_Q13976.

PharmGKB

PA33777.

GenAtlas

Search...

eggNOG

COG0515.

HOGENOM

HOG000233033.

HOVERGEN

HBG006211.

InParanoid

P14619.

KO

K07376.

OMA

KXTHYEN.

OrthoDB

EOG4V9TQ7.

BRENDA

2.7.11.12. 2681.

Reactome

REACT_604. Hemostasis.
REACT_6900. Immune System.

ArrayExpress

Q13976.

Bgee

Q13976.

CleanEx

HS_PRKG1.

Genevestigator

Q13976.

GermOnline

ENSG00000185532. Homo sapiens.

Gene3D

2.60.120.10. 2 hits.

InterPro

IPR000961. AGC-kinase_C.
IPR016232. cGMP-dependent_protein_kinase.
IPR002374. cGMP_dep_kinase.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014710. RmlC-like_jellyroll.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF00027. cNMP_binding. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]

PIRSF

PIRSF000559. cGMP-dep_kinase. 1 hit.

PRINTS

PR00104. CGMPKINASE.

SMART

SM00100. cNMP. 2 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF51206. cNMP_binding. 2 hits.
SSF56112. Kinase_like. 1 hit.

PROSITE

PS51285. AGC_KINASE_CTER. 1 hit.
PS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

BindingDB

Q13976.

ChEMBL

CHEMBL4273.

ChiTaRS

PRKG1. human.

EvolutionaryTrace

Q13976.

GenomeRNAi

5592.

NextBio

21698.

SOURCE

Search...

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Alpha (identifier: Q13976-1)

Also known as: CGK1-alpha;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Beta (identifier: Q13976-2)

Also known as: CGK1-beta;

The sequence of this isoform differs from the canonical sequence as follows:
1-89: MSELEEDFAK...AFRKFTKSER → MGTLRDLQYA...TLPFYPKSPQ

Entry name

KGP1_HUMAN

Accession

Primary (citable) accession number: Q13976
Secondary accession number(s): E2PU10

Q6P5T7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 131 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.