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Q13976 (KGP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length671 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 betaof PRKG1. Interacts with TRPC7 (via ankyrin repeat domain). Isoform alphainteracts with RGS2. Interacts with GTF2I. Ref.9 Ref.11 Ref.13 Ref.15 Ref.16 Ref.17 Ref.21 Ref.23 Ref.24

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.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.27

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.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseAortic aneurysm
Disease mutation
   DomainCoiled coil
   LigandATP-binding
cGMP
cGMP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Traceable author statement PubMed 10851246. Source: ProtInc

blood coagulation

Traceable author statement. Source: Reactome

dendrite development

Inferred from electronic annotation. Source: Ensembl

forebrain development

Inferred from electronic annotation. Source: Ensembl

negative regulation of platelet aggregation

Inferred from mutant phenotype Ref.15. Source: UniProtKB

neuron migration

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Traceable author statement PubMed 10851246. Source: ProtInc

regulation of GTPase activity

Inferred from mutant phenotype Ref.13. Source: UniProtKB

signal transduction

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.21. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

plasma membrane

Inferred from direct assay Ref.21Ref.15. Source: UniProtKB

   Molecular_functionATP 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...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BMPR2Q138732EBI-3952014,EBI-527196

Alternative products

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:
     2-89: SELEEDFAKI...AFRKFTKSER → MGTLRDLQYA...TLPFYPKSPQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 671670cGMP-dependent protein kinase 1
PRO_0000086115

Regions

Domain360 – 619260Protein kinase
Domain620 – 67152AGC-kinase C-terminal
Nucleotide binding167 – 1704cAMP or cGMP
Nucleotide binding177 – 1782cAMP or cGMP
Nucleotide binding366 – 3749ATP By similarity
Region2 – 102101Required for dimerization
Region9 – 4436Leucine-zipper
Region50 – 7526Autoinhibitory domain By similarity
Region103 – 220118cGMP-binding, high affinity
Region221 – 341121cGMP-binding, low affinity

Sites

Active site4841Proton acceptor By similarity
Binding site3901ATP By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.22
Modified residue591Phosphothreonine; by autocatalysis By similarity
Disulfide bond43Interchain By similarity

Natural variations

Alternative sequence2 – 8988SELEE…TKSER → MGTLRDLQYALQEKIEELRQ RDALIDELELELDQKDELIQ KLQNELDKYRSVIRPATQQA QKQSASTLQGEPRTKRQAIS AEPTAFDIQDLSHVTLPFYP KSPQ in isoform Beta.
VSP_038714
Natural variant1771R → Q in AAT8; impairs cGMP binding; the mutant protein is constitutively active. Ref.27
VAR_070434
Natural variant2491I → V. Ref.26
Corresponds to variant rs56082459 [ dbSNP | Ensembl ].
VAR_046773
Natural variant2671N → S. Ref.26
Corresponds to variant rs34997494 [ dbSNP | Ensembl ].
VAR_051632
Natural variant4741Y → F. Ref.27
VAR_070435
Natural variant6661G → A. Ref.27
VAR_070436

Experimental info

Mutagenesis121L → A: Loss of binding to PPP1R12A. Ref.9
Mutagenesis191I → A: Loss of binding to PPP1R12A. Ref.9
Mutagenesis261L → P: Loss of binding to PPP1R12A. Ref.9
Mutagenesis331I → A: Loss of binding to PPP1R12A. Ref.9
Mutagenesis401L → A: Loss of binding to PPP1R12A. Ref.9

Secondary structure

........................................................ 671
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha (CGK1-alpha) [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 51389502A5E5FBD2

FASTA67176,364
        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: 7A59FA64EE85C0C3
Show »

FASTA68777,935

References

« Hide '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. expand/collapse author list , 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.
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. expand/collapse author list , 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
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]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[23]"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.
[24]"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.
[25]"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.
[26]"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. expand/collapse author list , 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.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-249 AND SER-267.
[27]"Recurrent gain-of-function mutation in PRKG1 causes thoracic aortic aneurysms and acute aortic dissections."
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.
Am. J. Hum. Genet. 93:398-404(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AAT8 GLN-177, VARIANTS PHE-474 AND ALA-666, CHARACTERIZATION OF VARIANT AAT8 GLN-177.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y07512 mRNA. Translation: CAA68810.1.
D45864 mRNA. Translation: BAA08297.1.
Z92867 expand/collapse EMBL AC list , Z92869, Z92870, Z92871, Z92872, Z92873, Z92874, Z92875, Z92876, Z92877, Z92878, Z92879, Z92880, Z92881, Z92882, Z92883, Z92884, Z92885 Genomic DNA. Translation: CAB07436.1.
Z92868 expand/collapse EMBL AC list , Z92869, Z92870, Z92871, Z92872, Z92873, Z92874, Z92875, Z92876, Z92877, Z92878, Z92879, Z92880, Z92881, Z92882, Z92883, Z92884, Z92885 Genomic DNA. Translation: CAB07437.1.
AL391378 expand/collapse EMBL AC list , AC009986, AC022537, AC022025, AC027118, AL731537, AL928686, AL157399, AC026228 Genomic DNA. Translation: CAI39626.1.
AL928686 expand/collapse EMBL AC list , AC009986, AC022537, AL731537, AL391378, AL157399, AC027118, AC026228, AC022025 Genomic DNA. Translation: CAI40743.1.
AL157399 expand/collapse EMBL AC list , AC022025, AC009986, AL928686, AL731537, AL391378, AC027118, AC026228, AC022537 Genomic DNA. Translation: CAI41305.1.
AL731537 expand/collapse EMBL AC list , AL928686, AL391378, AL157399, AC027118, AC026228, AC022537, AC022025, AC009986 Genomic DNA. Translation: CAI17115.1.
CH471083 Genomic DNA. Translation: EAW54140.1.
BC062688 mRNA. Translation: AAH62688.1.
BC127090 mRNA. Translation: AAI27091.1.
PIRS05702.
RefSeqNP_001091982.1. NM_001098512.2.
NP_006249.1. NM_006258.3.
UniGeneHs.407535.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZXANMR-A/B2-58[»]
3NMDX-ray2.27A/B/C/D/E4-55[»]
3OCPX-ray2.49A/B92-227[»]
3OD0X-ray2.90A/B92-227[»]
3OGJX-ray2.75A/B/C/D92-219[»]
4KU7X-ray1.65A204-354[»]
4KU8X-ray1.99A/B/C204-354[»]
ProteinModelPortalQ13976.
SMRQ13976. Positions 9-660.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111578. 17 interactions.
DIPDIP-46288N.
IntActQ13976. 2 interactions.
MINTMINT-121708.
STRING9606.ENSP00000363092.

Chemistry

BindingDBQ13976.
ChEMBLCHEMBL4273.
GuidetoPHARMACOLOGY1492.

PTM databases

PhosphoSiteQ13976.

Polymorphism databases

DMDM6225588.

Proteomic databases

PaxDbQ13976.
PRIDEQ13976.

Protocols and materials databases

DNASU5592.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373980; ENSP00000363092; ENSG00000185532. [Q13976-2]
ENST00000401604; ENSP00000384200; ENSG00000185532. [Q13976-1]
GeneID5592.
KEGGhsa:5592.
UCSCuc001jjm.3. human. [Q13976-1]
uc001jjo.3. human. [Q13976-2]

Organism-specific databases

CTD5592.
GeneCardsGC10P052751.
HGNCHGNC:9414. PRKG1.
HPACAB009629.
HPA007699.
MIM176894. gene.
615436. phenotype.
neXtProtNX_Q13976.
Orphanet91387. Familial thoracic aortic aneurysm and aortic dissection.
PharmGKBPA33777.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233033.
HOVERGENHBG006211.
InParanoidP14619.
KOK07376.
OMAHQDLSRQ.
PhylomeDBQ13976.
TreeFamTF313261.

Enzyme and pathway databases

BRENDA2.7.11.12. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkQ13976.

Gene expression databases

ArrayExpressQ13976.
BgeeQ13976.
CleanExHS_PRKG1.
GenevestigatorQ13976.

Family and domain databases

Gene3D2.60.120.10. 2 hits.
InterProIPR000961. 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_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014710. RmlC-like_jellyroll.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00027. cNMP_binding. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFPIRSF000559. cGMP-dep_kinase. 1 hit.
PRINTSPR00104. CGMPKINASE.
SMARTSM00100. cNMP. 2 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF51206. SSF51206. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEPS51285. 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]
ProtoNetSearch...

Other

ChiTaRSPRKG1. human.
EvolutionaryTraceQ13976.
GeneWikiPRKG1.
GenomeRNAi5592.
NextBio21698.
PROQ13976.
SOURCESearch...

Entry information

Entry nameKGP1_HUMAN
AccessionPrimary (citable) accession number: Q13976
Secondary accession number(s): E2PU10 expand/collapse secondary AC list , P14619, Q5JSJ6, Q6P5T7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM