Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

cGMP-dependent protein kinase 1 (cGK 1) (cGK1) (EC 2.7.11.12) (cGMP-dependent protein kinase I) (cGKI)

 KGP1_HUMAN              Reviewed;         671 AA.
Q13976; A5YM56; B3KSF3; E2PU10; P14619; Q5JP05; Q5JSJ6; Q6P5T7;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 184.
RecName: Full=cGMP-dependent protein kinase 1;
Short=cGK 1;
Short=cGK1;
EC=2.7.11.12;
AltName: Full=cGMP-dependent protein kinase I;
Short=cGKI;
Name=PRKG1; Synonyms=PRKG1B, PRKGR1A, PRKGR1B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
TISSUE=Placenta;
PubMed=2792381; DOI=10.1016/0014-5793(89)81114-7;
Sandberg M., Natarajan V., Ronander I., Kalderon D., Walter U.,
Lohmann S.M., Jahnsen T.;
"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 Lett. 255:321-329(1989).
[2]
SEQUENCE REVISION.
Sandberg M.;
Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
TISSUE=Lung;
PubMed=8613202; DOI=10.1161/01.HYP.27.3.552;
Tamura N., Itoh H., Ogawa Y., Nakagawa O., Harada M., Chun T.,
Suga S., Yoshimasa T., Nakao K.;
"cDNA cloning and gene expression of human type Ialpha cGMP-dependent
protein kinase.";
Hypertension 27:552-557(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
PubMed=9192852; DOI=10.1006/geno.1997.4743;
Orstavik S., Natarajan V., Tasken K., Jahnsen T., Sandberg M.;
"Characterization of the human gene encoding the type I alpha and type
I beta cGMP-dependent protein kinase (PRKG1).";
Genomics 42:311-318(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
TISSUE=Cervix;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
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., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
FUNCTION IN PHOSPHORYLATION OF VASP.
PubMed=8182057;
Butt E., Abel K., Krieger M., Palm D., Hoppe V., Hoppe J., Walter U.;
"cAMP- and cGMP-dependent protein kinase phosphorylation sites of the
focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro
and in intact human platelets.";
J. Biol. Chem. 269:14509-14517(1994).
[11]
INTERACTION WITH PPP1R12A, SUBUNIT, MUTAGENESIS OF LEU-12; ILE-19;
LEU-26; ILE-33 AND LEU-40, AND FUNCTION.
PubMed=10567269; DOI=10.1126/science.286.5444.1583;
Surks H.K., Mochizuki N., Kasai Y., Georgescu S.P., Tang K.M., Ito M.,
Lincoln T.M., Mendelsohn M.E.;
"Regulation of myosin phosphatase by a specific interaction with cGMP-
dependent protein kinase Ialpha.";
Science 286:1583-1587(1999).
[12]
FUNCTION IN PHOSPHORYLATION OF RHOA.
PubMed=11162591; DOI=10.1006/bbrc.2000.4194;
Sawada N., Itoh H., Yamashita J., Doi K., Inoue M., Masatsugu K.,
Fukunaga Y., Sakaguchi S., Sone M., Yamahara K., Yurugi T., Nakao K.;
"cGMP-dependent protein kinase phosphorylates and inactivates RhoA.";
Biochem. Biophys. Res. Commun. 280:798-805(2001).
[13]
FUNCTION IN PHOSPHORYLATION OF GTF2I, AND INTERACTION WITH GTF2I.
PubMed=12082086; DOI=10.1074/jbc.M112332200;
Casteel D.E., Zhuang S., Gudi T., Tang J., Vuica M., Desiderio S.,
Pilz R.B.;
"cGMP-dependent protein kinase I beta physically and functionally
interacts with the transcriptional regulator TFII-I.";
J. Biol. Chem. 277:32003-32014(2002).
[14]
FUNCTION IN PHOSPHORYLATION OF PDE5.
PubMed=11723116; DOI=10.1074/jbc.M106562200;
Rybalkin S.D., Rybalkina I.G., Feil R., Hofmann F., Beavo J.A.;
"Regulation of cGMP-specific phosphodiesterase (PDE5) phosphorylation
in smooth muscle cells.";
J. Biol. Chem. 277:3310-3317(2002).
[15]
FUNCTION IN PHOSPHORYLATION OF RGS2, AND INTERACTION WITH RGS2.
PubMed=14608379; DOI=10.1038/nm958;
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.;
"Regulator of G-protein signaling-2 mediates vascular smooth muscle
relaxation and blood pressure.";
Nat. Med. 9:1506-1512(2003).
[16]
FUNCTION.
PubMed=15194681; DOI=10.1074/jbc.M405957200;
Wooldridge A.A., MacDonald J.A., Erdodi F., Ma C., Borman M.A.,
Hartshorne D.J., Haystead T.A.J.;
"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.";
J. Biol. Chem. 279:34496-34504(2004).
[17]
FUNCTION IN THE INHIBITION OF PLATELET AGGREGATION, FUNCTION IN
PHOSPHORYLATION OF MRVI1, SUBCELLULAR LOCATION, AND INTERACTION WITH
MRVI1 AND ITPR1.
PubMed=16990611; DOI=10.1182/blood-2005-10-026294;
Antl M., von Bruehl M.-L., Eiglsperger C., Werner M., Konrad I.,
Kocher T., Wilm M., Hofmann F., Massberg S., Schlossmann J.;
"IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation
and thrombus formation.";
Blood 109:552-559(2007).
[18]
INTERACTION WITH PPP1R12A.
PubMed=17904578; DOI=10.1016/j.jmb.2007.08.049;
Lee E., Hayes D.B., Langsetmo K., Sundberg E.J., Tao T.C.;
"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.";
J. Mol. Biol. 373:1198-1212(2007).
[19]
INTERACTION WITH PPP1R12A, AND SUBUNIT.
PubMed=18782776; DOI=10.1074/jbc.M804916200;
Sharma A.K., Zhou G.-P., Kupferman J., Surks H.K., Christensen E.N.,
Chou J.J., Mendelsohn M.E., Rigby A.C.;
"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.";
J. Biol. Chem. 283:32860-32869(2008).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[21]
REVIEW.
PubMed=20716671; DOI=10.1124/pr.110.002907;
Francis S.H., Busch J.L., Corbin J.D., Sibley D.;
"cGMP-dependent protein kinases and cGMP phosphodiesterases in nitric
oxide and cGMP action.";
Pharmacol. Rev. 62:525-563(2010).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
FUNCTION (ISOFORM ALPHA) IN PHOSPHORYLATION OF TRPC7, INTERACTION WITH
TRPC7, AND SUBCELLULAR LOCATION.
PubMed=21402151; DOI=10.1016/j.cellsig.2011.03.005;
Yuasa K., Matsuda T., Tsuji A.;
"Functional regulation of transient receptor potential canonical 7 by
cGMP-dependent protein kinase Ialpha.";
Cell. Signal. 23:1179-1187(2011).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[25]
STRUCTURE BY NMR OF 2-58, INTERACTION WITH PPP1R12A, SUBUNIT, AND
COILED-COIL.
PubMed=16131665; DOI=10.1110/ps.051528905;
Schnell J.R., Zhou G.-P., Zweckstetter M., Rigby A.C., Chou J.J.;
"Rapid and accurate structure determination of coiled-coil domains
using NMR dipolar couplings: application to cGMP-dependent protein
kinase Ialpha.";
Protein Sci. 14:2421-2428(2005).
[26]
X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 4-55 (ISOFORM BETA), AND
SUBUNIT.
PubMed=20826808; DOI=10.1074/jbc.C110.161430;
Casteel D.E., Smith-Nguyen E.V., Sankaran B., Roh S.H., Pilz R.B.,
Kim C.;
"A crystal structure of the cyclic GMP-dependent protein kinase
I{beta} dimerization/docking domain reveals molecular details of
isoform-specific anchoring.";
J. Biol. Chem. 285:32684-32688(2010).
[27]
X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 92-227 (ISOFORM BETA) IN
COMPLEX WITH CGMP AND CAMP.
PubMed=21526164; DOI=10.1371/journal.pone.0018413;
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.;
"Co-crystal structures of PKG Ibeta (92-227) with cGMP and cAMP reveal
the molecular details of cyclic-nucleotide binding.";
PLoS ONE 6:E18413-E18413(2011).
[28]
X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) OF 204-354 (ISOFORM BETA) IN
COMPLEX WITH CAMP AND CGMP.
PubMed=25271401; DOI=10.1021/bi501012v;
Huang G.Y., Gerlits O.O., Blakeley M.P., Sankaran B., Kovalevsky A.Y.,
Kim C.;
"Neutron diffraction reveals hydrogen bonds critical for cGMP-
selective activation: insights for cGMP-dependent protein kinase
agonist design.";
Biochemistry 53:6725-6727(2014).
[29]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 204-354 (ISOFORM BETA) IN
COMPLEX WITH CGMP, AND MUTAGENESIS OF LEU-281; ARG-282; THR-302 AND
TYR-336.
PubMed=24239458; DOI=10.1016/j.str.2013.09.021;
Huang G.Y., Kim J.J., Reger A.S., Lorenz R., Moon E.W., Zhao C.,
Casteel D.E., Bertinetti D., Vanschouwen B., Selvaratnam R.,
Pflugrath J.W., Sankaran B., Melacini G., Herberg F.W., Kim C.;
"Structural basis for cyclic-nucleotide selectivity and cGMP-selective
activation of PKG I.";
Structure 22:116-124(2014).
[30]
VARIANTS [LARGE SCALE ANALYSIS] VAL-249 AND SER-267.
PubMed=17344846; DOI=10.1038/nature05610;
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., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[31]
VARIANT AAT8 GLN-177, VARIANTS PHE-474 AND ALA-666, AND
CHARACTERIZATION OF VARIANT AAT8 GLN-177.
PubMed=23910461; DOI=10.1016/j.ajhg.2013.06.019;
GenTAC Registry Consortium;
National Heart, Lung, and Blood Institute Grand Opportunity Exome Sequencing Project;
Guo D.C., Regalado E., Casteel D.E., Santos-Cortez R.L., Gong L.,
Kim J.J., Dyack S., Horne S.G., Chang G., Jondeau G., Boileau C.,
Coselli J.S., Li Z., Leal S.M., Shendure J., Rieder M.J.,
Bamshad M.J., Nickerson D.A., Kim C., Milewicz D.M.;
"Recurrent gain-of-function mutation in PRKG1 causes thoracic aortic
aneurysms and acute aortic dissections.";
Am. J. Hum. Genet. 93:398-404(2013).
-!- 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 Ca(2+) release from intracellular stores, phosphorylation
of KCNMA1 (BKCa) channels decreases intracellular Ca(2+) 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.
{ECO:0000269|PubMed:10567269, ECO:0000269|PubMed:11162591,
ECO:0000269|PubMed:11723116, ECO:0000269|PubMed:12082086,
ECO:0000269|PubMed:14608379, ECO:0000269|PubMed:15194681,
ECO:0000269|PubMed:16990611, ECO:0000269|PubMed:8182057}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: In the absence of cGMP, PRKG1 activity is
suppressed by autoinhibitory contacts.
-!- SUBUNIT: 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. {ECO:0000250, ECO:0000269|PubMed:10567269,
ECO:0000269|PubMed:12082086, ECO:0000269|PubMed:14608379,
ECO:0000269|PubMed:16131665, ECO:0000269|PubMed:16990611,
ECO:0000269|PubMed:17904578, ECO:0000269|PubMed:18782776,
ECO:0000269|PubMed:20826808, ECO:0000269|PubMed:21402151}.
-!- INTERACTION:
Q13873:BMPR2; NbExp=2; IntAct=EBI-3952014, EBI-527196;
Q86V42:FAM124A; NbExp=3; IntAct=EBI-3952014, EBI-744506;
P25791:LMO2; NbExp=3; IntAct=EBI-3952014, EBI-739696;
O76074:PDE5A; NbExp=4; IntAct=EBI-3952014, EBI-9023531;
O15015:ZNF646; NbExp=3; IntAct=EBI-3952014, EBI-745608;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Colocalized
with TRPC7 in the plasma membrane. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=Alpha; Synonyms=CGK1-alpha;
IsoId=Q13976-1; Sequence=Displayed;
Name=Beta; Synonyms=CGK1-beta;
IsoId=Q13976-2, P14619-1;
Sequence=VSP_038714;
Name=3;
IsoId=Q13976-3; Sequence=VSP_055541, VSP_055542;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Primarily expressed in lung and placenta.
{ECO:0000269|PubMed:9192852}.
-!- 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.
-!- DOMAIN: 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.
-!- PTM: Autophosphorylation increases kinase activity.
-!- PTM: 65 kDa monomer is produced by proteolytic cleavage.
{ECO:0000250}.
-!- DISEASE: Aortic aneurysm, familial thoracic 8 (AAT8) [MIM:615436]:
A disease characterized by permanent dilation of the thoracic
aorta usually due to degenerative changes in the aortic wall. It
is primarily associated with a characteristic histologic
appearance known as 'medial necrosis' or 'Erdheim cystic medial
necrosis' in which there is degeneration and fragmentation of
elastic fibers, loss of smooth muscle cells, and an accumulation
of basophilic ground substance. {ECO:0000269|PubMed:23910461}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. cGMP subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y07512; CAA68810.1; -; mRNA.
EMBL; D45864; BAA08297.1; -; mRNA.
EMBL; AK093436; BAG52715.1; -; mRNA.
EMBL; EF560730; ABQ59040.1; -; mRNA.
EMBL; Z92867; CAB07436.1; -; Genomic_DNA.
EMBL; Z92869; CAB07436.1; JOINED; Genomic_DNA.
EMBL; Z92870; CAB07436.1; JOINED; Genomic_DNA.
EMBL; Z92871; CAB07436.1; JOINED; Genomic_DNA.
EMBL; Z92872; CAB07436.1; JOINED; Genomic_DNA.
EMBL; Z92873; CAB07436.1; JOINED; Genomic_DNA.
EMBL; Z92874; CAB07436.1; JOINED; Genomic_DNA.
EMBL; Z92875; CAB07436.1; JOINED; Genomic_DNA.
EMBL; Z92876; CAB07436.1; JOINED; Genomic_DNA.
EMBL; Z92877; CAB07436.1; JOINED; Genomic_DNA.
EMBL; Z92878; CAB07436.1; JOINED; Genomic_DNA.
EMBL; Z92879; CAB07436.1; JOINED; Genomic_DNA.
EMBL; Z92880; CAB07436.1; JOINED; Genomic_DNA.
EMBL; Z92881; CAB07436.1; JOINED; Genomic_DNA.
EMBL; Z92882; CAB07436.1; JOINED; Genomic_DNA.
EMBL; Z92883; CAB07436.1; JOINED; Genomic_DNA.
EMBL; Z92884; CAB07436.1; JOINED; Genomic_DNA.
EMBL; Z92885; CAB07436.1; JOINED; Genomic_DNA.
EMBL; Z92868; CAB07437.1; -; Genomic_DNA.
EMBL; Z92869; CAB07437.1; JOINED; Genomic_DNA.
EMBL; Z92870; CAB07437.1; JOINED; Genomic_DNA.
EMBL; Z92871; CAB07437.1; JOINED; Genomic_DNA.
EMBL; Z92872; CAB07437.1; JOINED; Genomic_DNA.
EMBL; Z92873; CAB07437.1; JOINED; Genomic_DNA.
EMBL; Z92874; CAB07437.1; JOINED; Genomic_DNA.
EMBL; Z92875; CAB07437.1; JOINED; Genomic_DNA.
EMBL; Z92876; CAB07437.1; JOINED; Genomic_DNA.
EMBL; Z92877; CAB07437.1; JOINED; Genomic_DNA.
EMBL; Z92878; CAB07437.1; JOINED; Genomic_DNA.
EMBL; Z92879; CAB07437.1; JOINED; Genomic_DNA.
EMBL; Z92880; CAB07437.1; JOINED; Genomic_DNA.
EMBL; Z92881; CAB07437.1; JOINED; Genomic_DNA.
EMBL; Z92882; CAB07437.1; JOINED; Genomic_DNA.
EMBL; Z92883; CAB07437.1; JOINED; Genomic_DNA.
EMBL; Z92884; CAB07437.1; JOINED; Genomic_DNA.
EMBL; Z92885; CAB07437.1; JOINED; Genomic_DNA.
EMBL; AL391378; CAI39626.1; -; Genomic_DNA.
EMBL; AC009986; CAI39626.1; JOINED; Genomic_DNA.
EMBL; AC022537; CAI39626.1; JOINED; Genomic_DNA.
EMBL; AC022025; CAI39626.1; JOINED; Genomic_DNA.
EMBL; AC027118; CAI39626.1; JOINED; Genomic_DNA.
EMBL; AL731537; CAI39626.1; JOINED; Genomic_DNA.
EMBL; AL928686; CAI39626.1; JOINED; Genomic_DNA.
EMBL; AL157399; CAI39626.1; JOINED; Genomic_DNA.
EMBL; AC026228; CAI39626.1; JOINED; Genomic_DNA.
EMBL; AL928686; CAI40743.1; -; Genomic_DNA.
EMBL; AC009986; CAI40743.1; JOINED; Genomic_DNA.
EMBL; AC022537; CAI40743.1; JOINED; Genomic_DNA.
EMBL; AL731537; CAI40743.1; JOINED; Genomic_DNA.
EMBL; AL391378; CAI40743.1; JOINED; Genomic_DNA.
EMBL; AL157399; CAI40743.1; JOINED; Genomic_DNA.
EMBL; AC027118; CAI40743.1; JOINED; Genomic_DNA.
EMBL; AC026228; CAI40743.1; JOINED; Genomic_DNA.
EMBL; AC022025; CAI40743.1; JOINED; Genomic_DNA.
EMBL; AL157399; CAI41305.1; -; Genomic_DNA.
EMBL; AC022025; CAI41305.1; JOINED; Genomic_DNA.
EMBL; AC009986; CAI41305.1; JOINED; Genomic_DNA.
EMBL; AL928686; CAI41305.1; JOINED; Genomic_DNA.
EMBL; AL731537; CAI41305.1; JOINED; Genomic_DNA.
EMBL; AL391378; CAI41305.1; JOINED; Genomic_DNA.
EMBL; AC027118; CAI41305.1; JOINED; Genomic_DNA.
EMBL; AC026228; CAI41305.1; JOINED; Genomic_DNA.
EMBL; AC022537; CAI41305.1; JOINED; Genomic_DNA.
EMBL; AL731537; CAI17115.1; -; Genomic_DNA.
EMBL; AL928686; CAI17115.1; JOINED; Genomic_DNA.
EMBL; AL391378; CAI17115.1; JOINED; Genomic_DNA.
EMBL; AL157399; CAI17115.1; JOINED; Genomic_DNA.
EMBL; AC027118; CAI17115.1; JOINED; Genomic_DNA.
EMBL; AC026228; CAI17115.1; JOINED; Genomic_DNA.
EMBL; AC022537; CAI17115.1; JOINED; Genomic_DNA.
EMBL; AC022025; CAI17115.1; JOINED; Genomic_DNA.
EMBL; AC009986; CAI17115.1; JOINED; Genomic_DNA.
EMBL; AC068062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC069079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC073584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL596105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL607031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471083; EAW54140.1; -; Genomic_DNA.
EMBL; BC062688; AAH62688.1; -; mRNA.
EMBL; BC127090; AAI27091.1; -; mRNA.
CCDS; CCDS44399.1; -. [Q13976-1]
CCDS; CCDS7244.1; -. [Q13976-2]
PIR; S05702; S05702.
RefSeq; NP_001091982.1; NM_001098512.2. [Q13976-1]
RefSeq; NP_006249.1; NM_006258.3. [Q13976-2]
UniGene; Hs.407535; -.
PDB; 1ZXA; NMR; -; A/B=2-59.
PDB; 3NMD; X-ray; 2.27 A; A/B/C/D/E=4-47.
PDB; 3OCP; X-ray; 2.49 A; A/B=84-212.
PDB; 3OD0; X-ray; 2.90 A; A/B=84-212.
PDB; 3OGJ; X-ray; 2.75 A; A/B/C/D=84-212.
PDB; 4KU7; X-ray; 1.65 A; A=204-354.
PDB; 4KU8; X-ray; 1.99 A; A/B/C=204-354.
PDB; 4QX5; X-ray; 1.32 A; A=204-354.
PDB; 4QXK; Other; 2.20 A; A=204-354.
PDB; 4R4L; X-ray; 2.25 A; A/B/C=2-48.
PDB; 4R4M; X-ray; 1.92 A; A/B/C=2-48.
PDB; 4Z07; X-ray; 2.50 A; A/C/E=84-336.
PDB; 5J48; X-ray; 1.49 A; A/B=204-336.
PDB; 5JAX; X-ray; 1.49 A; A=204-336.
PDB; 5JD7; X-ray; 1.75 A; A=204-336.
PDB; 5L0N; X-ray; 1.28 A; A=204-336.
PDBsum; 1ZXA; -.
PDBsum; 3NMD; -.
PDBsum; 3OCP; -.
PDBsum; 3OD0; -.
PDBsum; 3OGJ; -.
PDBsum; 4KU7; -.
PDBsum; 4KU8; -.
PDBsum; 4QX5; -.
PDBsum; 4QXK; -.
PDBsum; 4R4L; -.
PDBsum; 4R4M; -.
PDBsum; 4Z07; -.
PDBsum; 5J48; -.
PDBsum; 5JAX; -.
PDBsum; 5JD7; -.
PDBsum; 5L0N; -.
ProteinModelPortal; Q13976; -.
SMR; Q13976; -.
BioGrid; 111578; 26.
DIP; DIP-41118N; -.
DIP; DIP-46288N; -.
IntAct; Q13976; 10.
MINT; Q13976; -.
BindingDB; Q13976; -.
ChEMBL; CHEMBL4273; -.
GuidetoPHARMACOLOGY; 1492; -.
iPTMnet; Q13976; -.
PhosphoSitePlus; Q13976; -.
BioMuta; PRKG1; -.
DMDM; 6225588; -.
EPD; Q13976; -.
MaxQB; Q13976; -.
PeptideAtlas; Q13976; -.
PRIDE; Q13976; -.
DNASU; 5592; -.
Ensembl; ENST00000373980; ENSP00000363092; ENSG00000185532. [Q13976-2]
Ensembl; ENST00000373985; ENSP00000363097; ENSG00000185532. [Q13976-1]
GeneID; 5592; -.
KEGG; hsa:5592; -.
UCSC; uc001jjo.4; human. [Q13976-1]
CTD; 5592; -.
DisGeNET; 5592; -.
EuPathDB; HostDB:ENSG00000185532.15; -.
GeneCards; PRKG1; -.
HGNC; HGNC:9414; PRKG1.
HPA; CAB009629; -.
HPA; HPA007699; -.
MalaCards; PRKG1; -.
MIM; 176894; gene.
MIM; 615436; phenotype.
neXtProt; NX_Q13976; -.
OpenTargets; ENSG00000185532; -.
Orphanet; 91387; Familial thoracic aortic aneurysm and aortic dissection.
PharmGKB; PA33777; -.
GeneTree; ENSGT00810000125385; -.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG006211; -.
InParanoid; Q13976; -.
KO; K07376; -.
OMA; EPQTHQD; -.
OrthoDB; EOG091G0S9R; -.
PhylomeDB; Q13976; -.
TreeFam; TF313261; -.
BRENDA; 2.7.11.12; 2681.
Reactome; R-HSA-392517; Rap1 signalling.
Reactome; R-HSA-4086398; Ca2+ pathway.
Reactome; R-HSA-418457; cGMP effects.
SABIO-RK; Q13976; -.
SignaLink; Q13976; -.
SIGNOR; Q13976; -.
ChiTaRS; PRKG1; human.
EvolutionaryTrace; Q13976; -.
GeneWiki; PRKG1; -.
GenomeRNAi; 5592; -.
PRO; PR:Q13976; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000185532; -.
CleanEx; HS_PRKG1; -.
ExpressionAtlas; Q13976; baseline and differential.
Genevisible; Q13976; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005246; F:calcium channel regulator activity; IDA:UniProtKB.
GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
GO; GO:0004692; F:cGMP-dependent protein kinase activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004672; F:protein kinase activity; IMP:BHF-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
GO; GO:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
GO; GO:0019934; P:cGMP-mediated signaling; IEA:Ensembl.
GO; GO:0016358; P:dendrite development; IEA:Ensembl.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0090331; P:negative regulation of platelet aggregation; IMP:UniProtKB.
GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IDA:BHF-UCL.
GO; GO:1904706; P:negative regulation of vascular smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0043087; P:regulation of GTPase activity; IMP:UniProtKB.
GO; GO:0060087; P:relaxation of vascular smooth muscle; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd00038; CAP_ED; 2.
CDD; cd05572; STKc_cGK; 1.
Gene3D; 2.60.120.10; -; 2.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR002374; cGMP_dep_kinase.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR018488; cNMP-bd_CS.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR031831; PKcGMP_CC.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR014710; RmlC-like_jellyroll.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR035014; STKc_cGK.
Pfam; PF00027; cNMP_binding; 2.
Pfam; PF16808; PKcGMP_CC; 1.
Pfam; PF00069; Pkinase; 1.
PIRSF; PIRSF000559; cGMP-dep_kinase; 1.
PRINTS; PR00104; CGMPKINASE.
SMART; SM00100; cNMP; 2.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF51206; SSF51206; 2.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00888; CNMP_BINDING_1; 2.
PROSITE; PS00889; CNMP_BINDING_2; 2.
PROSITE; PS50042; CNMP_BINDING_3; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Allosteric enzyme; Alternative splicing;
Aortic aneurysm; ATP-binding; cGMP; cGMP-binding; Coiled coil;
Complete proteome; Cytoplasm; Disease mutation; Disulfide bond;
Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism;
Reference proteome; Serine/threonine-protein kinase; Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 671 cGMP-dependent protein kinase 1.
/FTId=PRO_0000086115.
DOMAIN 360 619 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 620 671 AGC-kinase C-terminal.
NP_BIND 167 170 cAMP or cGMP 1. {ECO:0000244|PDB:3OCP,
ECO:0000244|PDB:3OD0,
ECO:0000244|PDB:3OGJ,
ECO:0000269|PubMed:21526164}.
NP_BIND 177 178 cAMP or cGMP 1. {ECO:0000244|PDB:3OCP,
ECO:0000244|PDB:3OD0,
ECO:0000244|PDB:3OGJ,
ECO:0000269|PubMed:21526164}.
NP_BIND 291 294 cAMP or cGMP 2. {ECO:0000244|PDB:4KU7,
ECO:0000244|PDB:4QX5,
ECO:0000244|PDB:4QXK,
ECO:0000269|PubMed:24239458,
ECO:0000269|PubMed:25271401}.
NP_BIND 301 302 cAMP or cGMP 2. {ECO:0000244|PDB:4KU7,
ECO:0000244|PDB:4QX5,
ECO:0000244|PDB:4QXK,
ECO:0000269|PubMed:24239458,
ECO:0000269|PubMed:25271401}.
NP_BIND 366 374 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 2 102 Required for dimerization.
REGION 9 44 Leucine-zipper.
REGION 50 75 Autoinhibitory domain. {ECO:0000250}.
REGION 103 220 cGMP-binding, high affinity.
REGION 221 341 cGMP-binding, low affinity.
COILED 2 59 {ECO:0000269|PubMed:16131665}.
ACT_SITE 484 484 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 282 282 cGMP 2. {ECO:0000244|PDB:4KU7,
ECO:0000244|PDB:4QX5,
ECO:0000244|PDB:4QXK,
ECO:0000269|PubMed:24239458,
ECO:0000269|PubMed:25271401}.
BINDING 336 336 cAMP or cGMP 2. {ECO:0000244|PDB:4KU7,
ECO:0000244|PDB:4QX5,
ECO:0000244|PDB:4QXK,
ECO:0000269|PubMed:24239458,
ECO:0000269|PubMed:25271401}.
BINDING 390 390 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 59 59 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:P00516}.
MOD_RES 515 515 Phosphothreonine.
{ECO:0000250|UniProtKB:P0C605}.
DISULFID 43 43 Interchain. {ECO:0000250}.
VAR_SEQ 1 89 MSELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLH
KCQSVLPVPSTHIGPRTTRAQGISAEPQTYRSFHDLRQAFR
KFTKSER -> MGTLRDLQYALQEKIEELRQRDALIDELEL
ELDQKDELIQKLQNELDKYRSVIRPATQQAQKQSASTLQGE
PRTKRQAISAEPTAFDIQDLSHVTLPFYPKSPQ (in
isoform Beta).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:2792381}.
/FTId=VSP_038714.
VAR_SEQ 1 15 MSELEEDFAKILMLK -> MEKQNMFLHGSYILR (in
isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055541.
VAR_SEQ 16 297 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055542.
VARIANT 177 177 R -> Q (in AAT8; impairs cGMP binding;
the mutant protein is constitutively
active; dbSNP:rs397515330).
{ECO:0000269|PubMed:23910461}.
/FTId=VAR_070434.
VARIANT 249 249 I -> V (in dbSNP:rs56082459).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_046773.
VARIANT 267 267 N -> S (in dbSNP:rs34997494).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_051632.
VARIANT 474 474 Y -> F (in dbSNP:rs149710600).
{ECO:0000269|PubMed:23910461}.
/FTId=VAR_070435.
VARIANT 666 666 G -> A (in dbSNP:rs750949508).
{ECO:0000269|PubMed:23910461}.
/FTId=VAR_070436.
MUTAGEN 12 12 L->A: Loss of binding to PPP1R12A.
{ECO:0000269|PubMed:10567269}.
MUTAGEN 19 19 I->A: Loss of binding to PPP1R12A.
{ECO:0000269|PubMed:10567269}.
MUTAGEN 26 26 L->P: Loss of binding to PPP1R12A.
{ECO:0000269|PubMed:10567269}.
MUTAGEN 33 33 I->A: Loss of binding to PPP1R12A.
{ECO:0000269|PubMed:10567269}.
MUTAGEN 40 40 L->A: Loss of binding to PPP1R12A.
{ECO:0000269|PubMed:10567269}.
MUTAGEN 281 281 L->A: Reduces cGMP binding affinity.
{ECO:0000269|PubMed:24239458}.
MUTAGEN 282 282 R->A: Reduces cGMP binding affinity.
{ECO:0000269|PubMed:24239458}.
MUTAGEN 302 302 T->A: Reduces cGMP binding affinity.
{ECO:0000269|PubMed:24239458}.
MUTAGEN 336 336 Y->A: Reduces cGMP binding affinity.
{ECO:0000269|PubMed:24239458}.
HELIX 3 44 {ECO:0000244|PDB:4R4M}.
HELIX 88 100 {ECO:0000244|PDB:3OCP}.
TURN 102 106 {ECO:0000244|PDB:3OCP}.
HELIX 109 118 {ECO:0000244|PDB:3OCP}.
STRAND 120 124 {ECO:0000244|PDB:3OCP}.
STRAND 129 131 {ECO:0000244|PDB:3OCP}.
STRAND 139 145 {ECO:0000244|PDB:3OCP}.
STRAND 148 152 {ECO:0000244|PDB:3OCP}.
STRAND 155 160 {ECO:0000244|PDB:3OCP}.
STRAND 165 167 {ECO:0000244|PDB:3OCP}.
HELIX 169 173 {ECO:0000244|PDB:3OCP}.
STRAND 174 176 {ECO:0000244|PDB:3OD0}.
STRAND 178 185 {ECO:0000244|PDB:3OCP}.
STRAND 187 193 {ECO:0000244|PDB:3OCP}.
HELIX 194 201 {ECO:0000244|PDB:3OCP}.
HELIX 209 217 {ECO:0000244|PDB:5L0N}.
HELIX 220 222 {ECO:0000244|PDB:5L0N}.
HELIX 227 236 {ECO:0000244|PDB:5L0N}.
STRAND 238 242 {ECO:0000244|PDB:5L0N}.
STRAND 247 249 {ECO:0000244|PDB:5L0N}.
STRAND 257 264 {ECO:0000244|PDB:5L0N}.
STRAND 266 270 {ECO:0000244|PDB:5L0N}.
STRAND 274 276 {ECO:0000244|PDB:4KU8}.
STRAND 279 284 {ECO:0000244|PDB:5L0N}.
HELIX 292 296 {ECO:0000244|PDB:5L0N}.
STRAND 297 300 {ECO:0000244|PDB:4Z07}.
STRAND 303 317 {ECO:0000244|PDB:5L0N}.
HELIX 318 325 {ECO:0000244|PDB:5L0N}.
TURN 326 329 {ECO:0000244|PDB:5L0N}.
HELIX 330 349 {ECO:0000244|PDB:4KU8}.
SEQUENCE 671 AA; 76364 MW; 51389502A5E5FBD2 CRC64;
MSELEEDFAK ILMLKEERIK ELEKRLSEKE EEIQELKRKL HKCQSVLPVP STHIGPRTTR
AQGISAEPQT YRSFHDLRQA FRKFTKSERS KDLIKEAILD NDFMKNLELS QIQEIVDCMY
PVEYGKDSCI IKEGDVGSLV YVMEDGKVEV TKEGVKLCTM GPGKVFGELA ILYNCTRTAT
VKTLVNVKLW AIDRQCFQTI MMRTGLIKHT EYMEFLKSVP TFQSLPEEIL SKLADVLEET
HYENGEYIIR QGARGDTFFI ISKGTVNVTR EDSPSEDPVF LRTLGKGDWF GEKALQGEDV
RTANVIAAEA VTCLVIDRDS FKHLIGGLDD VSNKAYEDAE AKAKYEAEAA FFANLKLSDF
NIIDTLGVGG FGRVELVQLK SEESKTFAMK ILKKRHIVDT RQQEHIRSEK QIMQGAHSDF
IVRLYRTFKD SKYLYMLMEA CLGGELWTIL RDRGSFEDST TRFYTACVVE AFAYLHSKGI
IYRDLKPENL ILDHRGYAKL VDFGFAKKIG FGKKTWTFCG TPEYVAPEII LNKGHDISAD
YWSLGILMYE LLTGSPPFSG PDPMKTYNII LRGIDMIEFP KKIAKNAANL IKKLCRDNPS
ERLGNLKNGV KDIQKHKWFE GFNWEGLRKG TLTPPIIPSV ASPTDTSNFD SFPEDNDEPP
PDDNSGWDID F


Related products :

Catalog number Product name Quantity
82801-73-8 cGMP Dependent kinase inhibitor peptid cGMP Dependent Kina 1g
KGP2_RAT Rat ELISA Kit FOR cGMP-dependent protein kinase 2 96T
CSB-EL018716RA Rat cGMP-dependent protein kinase 2(PRKG2) ELISA kit 96T
KGP2_HUMAN Human ELISA Kit FOR cGMP-dependent protein kinase 2 96T
EH3652 Protein Kinase, cGMP Dependent Type I Elisa Kit 96T
CSB-EL018716MO Mouse cGMP-dependent protein kinase 2(PRKG2) ELISA kit 96T
CSB-EL018715MO Mouse cGMP-dependent protein kinase 1(PRKG1) ELISA kit 96T
CSB-EL018715HU Human cGMP-dependent protein kinase 1(PRKG1) ELISA kit 96T
E97314Hu ELISA Kit for Protein Kinase, cGMP Dependent Type I (PRKG1) 96T/Kit
E13242h Human Protein Kinase, cGMP Dependent Type II ELISA 96T
PRKRA PRKG1 Gene protein kinase, cGMP-dependent, type I
PRKRIP1 PRKG2 Gene protein kinase, cGMP-dependent, type II
G0871 PRKG1 (Protein Kinase, cGMP Dependent Type I), Pig, ELISA Kit 96T
CSB-EL018715BO Bovine cGMP-dependent protein kinase 1(PRKG1) ELISA kit 96T
CSB-EL018716HU Human cGMP-dependent protein kinase 2(PRKG2) ELISA kit 96T
CSB-EL018716RA Rat cGMP-dependent protein kinase 2(PRKG2) ELISA kit SpeciesRat 96T
CSB-EL018716HU Human cGMP-dependent protein kinase 2(PRKG2) ELISA kit SpeciesHuman 96T
G0868 PRKG1 (Protein Kinase, cGMP Dependent Type I), Guinea Pig, ELISA Kit 96T
UB-E05051 Human Protein Kinase, cGMP Dependent Type I(PRKG1)ELISA Kit 96T
CSB-EL018715RB Rabbit cGMP-dependent protein kinase 1(PRKG1) ELISA kit SpeciesRabbit 96T
CSB-EL018716MO Mouse cGMP-dependent protein kinase 2(PRKG2) ELISA kit SpeciesMouse 96T
QY-E05051 Human Protein Kinase, cGMP Dependent Type I(PRKG1)ELISA Kit 96T
CSB-EL018715MO Mouse cGMP-dependent protein kinase 1(PRKG1) ELISA kit SpeciesMouse 96T
G0872 PRKG1 (Protein Kinase, cGMP Dependent Type I), Rabbit, ELISA Kit 96T
CSB-EL018715HU Human cGMP-dependent protein kinase 1(PRKG1) ELISA kit SpeciesHuman 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur