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

 KGP1_MOUSE              Reviewed;         671 AA.
P0C605; Q14DK6; Q9Z0Z0;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
15-JAN-2008, sequence version 1.
05-DEC-2018, entry version 107.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=10085070; DOI=10.1074/jbc.274.13.8391;
Collins S.P., Uhler M.D.;
"Cyclic AMP- and cyclic GMP-dependent protein kinases differ in their
regulation of cyclic AMP response element-dependent gene
transcription.";
J. Biol. Chem. 274:8391-8404(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
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).
[4]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=9606187; DOI=10.1093/emboj/17.11.3045;
Pfeifer A., Klatt P., Massberg S., Ny L., Sausbier M., Hirneiss C.,
Wang G.X., Korth M., Aszodi A., Andersson K.E., Krombach F.,
Mayerhofer A., Ruth P., Fassler R., Hofmann F.;
"Defective smooth muscle regulation in cGMP kinase I-deficient mice.";
EMBO J. 17:3045-3051(1998).
[5]
FUNCTION IN PHOSPHORYLATION OF PPP1R17.
TISSUE=Brain;
PubMed=9920894; DOI=10.1074/jbc.274.6.3485;
Hall K.U., Collins S.P., Gamm D.M., Massa E., Depaoli-Roach A.A.,
Uhler M.D.;
"Phosphorylation-dependent inhibition of protein phosphatase-1 by G-
substrate: a Purkinje cell substrate of the cyclic GMP-dependent
protein kinase.";
J. Biol. Chem. 274:3485-3495(1999).
[6]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=10209042; DOI=10.1084/jem.189.8.1255;
Massberg S., Sausbier M., Klatt P., Bauer M., Pfeifer A., Siess W.,
Fassler R., Ruth P., Krombach F., Hofmann F.;
"Increased adhesion and aggregation of platelets lacking cyclic
guanosine 3',5'-monophosphate kinase I.";
J. Exp. Med. 189:1255-1264(1999).
[7]
FUNCTION IN THE REGULATION OF VASCULAR TONE.
PubMed=11055988; DOI=10.1161/01.RES.87.9.825;
Sausbier M., Schubert R., Voigt V., Hirneiss C., Pfeifer A., Korth M.,
Kleppisch T., Ruth P., Hofmann F.;
"Mechanisms of NO/cGMP-dependent vasorelaxation.";
Circ. Res. 87:825-830(2000).
[8]
TISSUE SPECIFICITY.
PubMed=16154279; DOI=10.1016/j.neuroscience.2005.06.051;
Feil S., Zimmermann P., Knorn A., Brummer S., Schlossmann J.,
Hofmann F., Feil R.;
"Distribution of cGMP-dependent protein kinase type I and its isoforms
in the mouse brain and retina.";
Neuroscience 135:863-868(2005).
[9]
INTERACTION WITH MRVI1.
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).
[10]
FUNCTION.
PubMed=19156199; DOI=10.1371/journal.pone.0004238;
Langmesser S., Franken P., Feil S., Emmenegger Y., Albrecht U.,
Feil R.;
"cGMP-dependent protein kinase type I is implicated in the regulation
of the timing and quality of sleep and wakefulness.";
PLoS ONE 4:E4238-E4238(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-515, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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:10209042, ECO:0000269|PubMed:11055988,
ECO:0000269|PubMed:19156199, ECO:0000269|PubMed:9606187,
ECO:0000269|PubMed:9920894}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
EC=2.7.11.12;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.12;
-!- ACTIVITY REGULATION: In the absence of cGMP, PRKG1 activity is
suppressed by autoinhibitory contacts. {ECO:0000250}.
-!- 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 (By similarity). 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 (By similarity). Interacts
with TRPC7 (via ankyrin repeat domain) (By similarity). Isoform
alpha interacts with RGS2 (By similarity). Interacts with GTF2I
(By similarity). {ECO:0000250}.
-!- INTERACTION:
O35607:Bmpr2; NbExp=4; IntAct=EBI-6991999, EBI-527224;
Q9DBR7:Ppp1r12a; NbExp=2; IntAct=EBI-15699851, EBI-1014335;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Colocalized
with TRPC7 in the plasma membrane. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Alpha; Synonyms=CGK1-alpha;
IsoId=P0C605-1; Sequence=Displayed;
Name=Beta; Synonyms=CGK1-beta;
IsoId=P0C605-2, Q9Z0Z0-1;
Sequence=VSP_038715;
-!- TISSUE SPECIFICITY: Detected in cerebellum, hippocampus,
dorsomedial hypothalamus, medulla, subcommissural organ, cerebral
cortex, amygdala, habenulae, various hypothalamic regions,
olfactory bulb, pituitary gland, and retina. Isoform alpha is
prominent in the cerebellum and medulla, whereas isoform Beta is
predominant in the cortex, hippocampus, hypothalamus, and
olfactory bulb. {ECO:0000269|PubMed:16154279}.
-!- 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 (By similarity). {ECO:0000250}.
-!- 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. {ECO:0000250}.
-!- PTM: Autophosphorylation increases kinase activity. {ECO:0000250}.
-!- PTM: 65 kDa monomer is produced by proteolytic cleavage.
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Leads to premature death at approximately 6
weeks of age, presumably due to smooth muscle dysfunction. These
mice show multiple defects including impaired smooth muscle
relaxation, disturbed gastrointestinal motility and enhanced
platelet adhesion. {ECO:0000269|PubMed:10209042,
ECO:0000269|PubMed:9606187}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. cGMP subfamily. {ECO:0000305}.
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EMBL; AF084547; AAD16044.1; -; mRNA.
EMBL; AC102751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC103405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC108399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC116507; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC119158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC122548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC113162; AAI13163.1; -; mRNA.
CCDS; CCDS29745.1; -. [P0C605-1]
CCDS; CCDS29746.1; -. [P0C605-2]
RefSeq; NP_001013855.1; NM_001013833.3. [P0C605-1]
RefSeq; NP_035290.1; NM_011160.3. [P0C605-2]
RefSeq; XP_006526831.1; XM_006526768.3. [P0C605-1]
UniGene; Mm.381170; -.
ProteinModelPortal; P0C605; -.
SMR; P0C605; -.
BioGrid; 202372; 3.
DIP; DIP-29981N; -.
IntAct; P0C605; 5.
MINT; P0C605; -.
iPTMnet; P0C605; -.
PhosphoSitePlus; P0C605; -.
PeptideAtlas; P0C605; -.
PRIDE; P0C605; -.
Ensembl; ENSMUST00000065067; ENSMUSP00000067576; ENSMUSG00000052920. [P0C605-1]
Ensembl; ENSMUST00000073581; ENSMUSP00000073268; ENSMUSG00000052920. [P0C605-2]
GeneID; 19091; -.
KEGG; mmu:19091; -.
UCSC; uc008heo.2; mouse. [P0C605-2]
UCSC; uc008hep.2; mouse. [P0C605-1]
CTD; 5592; -.
MGI; MGI:108174; Prkg1.
GeneTree; ENSGT00940000154704; -.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG006211; -.
InParanoid; P0C605; -.
KO; K07376; -.
OMA; KGETYAE; -.
OrthoDB; EOG091G0S9R; -.
PhylomeDB; P0C605; -.
TreeFam; TF313261; -.
BRENDA; 2.7.11.12; 3474.
Reactome; R-MMU-392517; Rap1 signalling.
Reactome; R-MMU-418457; cGMP effects.
ChiTaRS; Prkg1; mouse.
PRO; PR:P0C605; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000052920; Expressed in 177 organ(s), highest expression level in epithelium of lens.
CleanEx; MM_PRKG1; -.
ExpressionAtlas; P0C605; baseline and differential.
Genevisible; P0C605; MM.
GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; ISS:UniProtKB.
GO; GO:0030553; F:cGMP binding; IDA:UniProtKB.
GO; GO:0004692; F:cGMP-dependent protein kinase activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; ISO:MGI.
GO; GO:0019934; P:cGMP-mediated signaling; IMP:MGI.
GO; GO:0016358; P:dendrite development; IMP:MGI.
GO; GO:0030900; P:forebrain development; IMP:MGI.
GO; GO:0014050; P:negative regulation of glutamate secretion; ISO:MGI.
GO; GO:0045822; P:negative regulation of heart contraction; ISO:MGI.
GO; GO:0010920; P:negative regulation of inositol phosphate biosynthetic process; ISO:MGI.
GO; GO:0090331; P:negative regulation of platelet aggregation; ISS:UniProtKB.
GO; GO:0014912; P:negative regulation of smooth muscle cell migration; ISO:MGI.
GO; GO:0045986; P:negative regulation of smooth muscle contraction; IMP:MGI.
GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; ISO:MGI.
GO; GO:1904706; P:negative regulation of vascular smooth muscle cell proliferation; ISO:MGI.
GO; GO:0001764; P:neuron migration; IMP:MGI.
GO; GO:0097755; P:positive regulation of blood vessel diameter; ISO:MGI.
GO; GO:0042753; P:positive regulation of circadian rhythm; ISO:MGI.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
GO; GO:1902608; P:positive regulation of large conductance calcium-activated potassium channel activity; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
GO; GO:2000224; P:regulation of testosterone biosynthetic process; ISO:MGI.
GO; GO:0060087; P:relaxation of vascular smooth muscle; IMP:MGI.
GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
CDD; cd00038; CAP_ED; 2.
CDD; cd05572; STKc_cGK; 1.
Gene3D; 2.60.120.10; -; 2.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR039811; cAMP/cGMP-dep_PK.
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.
PANTHER; PTHR24353; PTHR24353; 1.
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;
Acetylation; Allosteric enzyme; Alternative splicing; ATP-binding;
cGMP; cGMP-binding; Coiled coil; Complete proteome; Cytoplasm;
Disulfide bond; Kinase; Nucleotide-binding; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P00516}.
CHAIN 2 671 cGMP-dependent protein kinase 1.
/FTId=PRO_0000314022.
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:0000250|UniProtKB:Q13976}.
NP_BIND 177 178 cAMP or cGMP 1.
{ECO:0000250|UniProtKB:Q13976}.
NP_BIND 291 294 cAMP or cGMP 2.
{ECO:0000250|UniProtKB:Q13976}.
NP_BIND 301 302 cAMP or cGMP 2.
{ECO:0000250|UniProtKB:Q13976}.
NP_BIND 366 374 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 2 102 Required for dimerization. {ECO:0000250}.
REGION 9 44 Leucine-zipper.
REGION 50 75 Autoinhibitory domain. {ECO:0000250}.
REGION 103 220 cGMP-binding, high affinity.
{ECO:0000250}.
REGION 221 341 cGMP-binding, low affinity.
{ECO:0000250}.
COILED 2 59 {ECO:0000250}.
ACT_SITE 484 484 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 282 282 cGMP 2. {ECO:0000250|UniProtKB:Q13976}.
BINDING 336 336 cAMP or cGMP 2.
{ECO:0000250|UniProtKB:Q13976}.
BINDING 390 390 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P00516}.
MOD_RES 59 59 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:P00516}.
MOD_RES 515 515 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
DISULFID 43 43 Interchain. {ECO:0000250}.
VAR_SEQ 1 89 MSELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLH
KCQSVLPVPSTHIGPRTTRAQGISAEPQTYRSFHDLRQAFR
KFTKSER -> MGTLRDLQYALQEKIEELRQRDALIDELEL
ELDQKDELIQKLQNELDKYRSVIRPATQQAQKQSASTLQGE
PRTKRQAISAEPTAFDIQDLSHVTLPFYPKSPQ (in
isoform Beta).
{ECO:0000303|PubMed:10085070,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_038715.
SEQUENCE 671 AA; 76350 MW; 51878E2D27F26A22 CRC64;
MSELEEDFAK ILMLKEERIK ELEKRLSEKE EEIQELKRKL HKCQSVLPVP STHIGPRTTR
AQGISAEPQT YRSFHDLRQA FRKFTKSERS KDLIKEAILD NDFMKNLELS QIQEIVDCMY
PVEYGKDSCI IKEGDVGSLV YVMEDGKVEV TKEGVKLCTM GPGKVFGELA ILYNCTRTAT
VKTLVNVKLW AIDRQCFQTI MMRTGLIKHT EYMEFLKSVP TFQSLPDEIL SKLADVLEET
HYENGEYIIR QGARGDTFFI ISKGQVNVTR 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 SFPEDSDEPP
PDDNSGWDID F


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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


 

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