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0KGP1B_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePRKG1
Descriptioncgmp-dependent protein kinase 1, beta isozyme (ec 2.7.1.37) (cgk 1 beta) (cgki-beta).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0030036 actin cytoskeleton organization and biogenesis (TAS)
0006468 protein amino acid phosphorylation (TAS)
0007165 signal transduction (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Eukaryotic protein kinases are enzymesthat belong to a very extensive family of proteins which share a conserved catalytic core common withboth serine/threonine and tyrosine protein kinases. There are a number of conserved regions in thecatalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is aglycine-rich stretch of residues in the vicinity of a lysine residue.hich has been shown to be involvedin ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residuewhich is important for the catalytic activity of the enzyme . CAUTION: Despite SMART having created two different HMMs for Serine/Threonine protein kinase and for Tyrosine protein kinase.arge number of proteins match both signatures.s SMART considers it to be natural for these two closely related families.
  IPR002290:Serine/threonine protein kinase
Proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues . The best studied of these proteins is the prokaryotic catabolite gene activator (alsoknown as the cAMP receptor protein) (gene crp) where such a domain is known to be composed of three alpha-helices anda distinctive eight-stranded.ntiparallel beta-barrel structure. There are six invariant amino acids in this domain.hree of which are glycine residues that are thought to be essential for maintenance of the structural integrity ofthe beta-barrel. cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclicnucleotide-binding domain. The cAPKs are composed of two different subunits. catalytic chain and a regulatory chain.hich contains both copies of the domain. The cGPKs are single chain enzymes that include the two copies of the domainin their N-terminal section. Vertebrate cyclic nucleotide-gated ion-channels also contain this domain. Two suchcations channels have been fully characterized.ne is found in rod cells where it plays a role in visual signaltransduction.
  IPR000595:Cyclic nucleotide-binding
Protein kinases are responsible for the phosphorylation of proteins.otentially for regulating their activity. This domain is found in a large variety of protein kinases with different functions and dependencies. Protein kinase C.or example.s a calcium-activated.hospholipid-dependent serine- and threonine-specific enzyme. It is activated by diacylglycerol which.n turn.hosphorylates a range ofcellular proteins. This domain is most often found associated with .
  IPR000961:Protein kinase, C-terminal
Eukaryotic protein kinases are enzymesthat belong to a very extensive family of proteins which share a conserved catalytic core common withboth serine/threonine and tyrosine protein kinases. There are a number of conserved regions in thecatalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is aglycine-rich stretch of residues in the vicinity of a lysine residue.hich has been shown to be involvedin ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residuewhich is important for the catalytic activity of the enzyme . This entry includes protein kinases from eukaryotes and viruses and may include some bacterial hits too.
  IPR000719:Protein kinase
Cyclic AMP (cAMP) is a key intracellular regulator of cell function in both prokaryotes and eukaryotes. One of the ways in which it regulates enzymes is by binding to and causing activation of cAMP-dependent protein kinases.hich in turn activate or deactivate other enzymes by phosphorylating them . In the absence of cAMP.rotein Kinase A (PKA) exists as an equimolar tetramer of regulatory (R) and catalytic (C) subunits . In addition to its role as an inhibitor of the C subunit.he R subunit anchors the holoenzyme to specific intracellular locations and prevents the C subunit from entering the nucleus. All R subunits have a conserved domain structure consisting of the N-terminal dimerization domain.nhibitory region.AMP-binding domain A and cAMP-binding domain B. R subunits interact with C subunits primarily through the inhibitory site. The cAMP-binding domains show extensive sequence similarity and bind cAMP cooperatively. Two types of R subunit exist - Type I and Type II - which differ in molecular weight.equence.utophosphorylation cabaility.ellular location and tissue distribution. Types I and II were further sub-divided into alpha and beta subtypes.ased mainly on sequence similarity. Type I does not undergo such autophosphorylation.ut it can be phosphorylated slowly in vitro by cGMP-dependent protein kinases . cAMP-dependent protein kinases are activated by the binding of two cAMP molecules to specific areas at the C-terminus of each regulatory subunit of the enzyme. This causes in a conformational change in the structure.esulting in dissociation of the active catalytic domain from the regulatory domains.
  IPR002373:cAMP-dependent protein kinase
Guanosine cyclase 3.-dependent protein kinases are known to play a role in smooth muscle relaxation.on fluxes in kidneys and intestines.nd neuronal function. The predominant form of cGMP-dependent protein kinase is a dimer of identical 75 kDa subunits.lthough larger subunits of 86 and 130 kDa have been found . The enzyme is kept in an inactive form by the interaction of the catalytic domain of one subunit with the region on the other subunit that precedes the cGMP binding domain. Each subunit contains two cGMP-binding regions.ound together in the sequence: binding of two molecules of cGMP precipitates a conformational change in the active site that allows the substrate to bind. Although cGMP- and cAMP-dependent protein kinases are similar both in structure and sequence around the nucleotide binding site.nd in the method of activation and inactivation.here are some basic contrasts. The major difference is that all of the functional domains of the cGMP- dependent enzymes are found on a single polypeptide chain.hereas cAMP- dependent protein kinases have separate regulatory (cAMP binding) and catalytic chains.
  IPR002374:cGMP-dependent protein kinase
Protein kinases () catalyze the phosphotransfer reaction fundamental to most signalling and regulatory processes in the eukaryotic cell . The catalytic subunit contains a core that is common to both serine/threonine and tyrosine protein kinases. The catalytic domain contains the nucleotide-binding site and the catalytic apparatus in an inter-lobe cleft. Structurally it shares functional and structural similarities with the ATP-grasp fold.hich is found in enzymes that catalyse the formation of an amide bond.nd with PIPK (phosphoinositol phosphate kinase). The three-dimensional fold of the protein kinase catalytic domain is similar to domains found in several other proteins. These include the catalytic domain of actin-fragmin kinase.n atypical protein kinase that regulates the F-actin capping activity in plasmodia ; the catalytic domain of phosphoinositide-3-kinase (PI3K).hich phosphorylates phosphoinositides and as such is involved in a number of fundamental cellular processes such as apoptosis.roliferation.otility and adhesion ; the catalytic domain of the MHCK/EF2 kinase.n atypical protein kinase that includes the TRP (transient channel potential) calcium-channel kinase involved in the modulation of calcium channels in eukaryotic cells in response to external signals ; choline kinase.hich catalyses the ATP-dependent phosphorylation of choline during the biosynthesis of phosphatidylcholine ; and 3.-aminoglycoside phosphotransferase type IIIa. bacterial enzyme that confers resistance to a range of aminoglycoside antibiotics .
  IPR011009:Protein kinase-like
IPR000719:Pkinase 
Evalue:-95.1079025268555 
Location:375-634IPR000595:cNMP 
Evalue:-32.8239087409443 
Location:236-358IPR000595:cNMP 
Evalue:-26.2006594505464 
Location:118-231IPR000961:S_TK_X 
Evalue:-10.2218487496164 
Location:635-686
SequencesProtein: KGP1B_HUMAN (686 aa)
mRNA: NM_006258
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
KO assignmentK07376
  Level 3 annotation:
    protein kinase, cGMP-dependent
  Level 2 annotation:
    Gap junction
    Long-term depression
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 96 residues, 52421123-52421410Exon2: 57 residues, 52582929-52583096Exon3: 40 residues, 52897488-52897602Exon4: 37 residues, 53234350-53234456Exon5: 23 residues, 53337272-53337336Exon6: 28 residues, 53484249-53484327Exon7: 33 residues, 53492302-53492397Exon8: 24 residues, 53563605-53563671Exon9: 27 residues, 53591654-53591729Exon10: 34 residues, 53681335-53681432Exon11: 48 residues, 53701115-53701255Exon12: 32 residues, 53702157-53702247Exon13: 49 residues, 53710554-53710696Exon14: 56 residues, 53711918-53712082Exon15: 43 residues, 53718491-53718614Exon16: 23 residues, 53718696-53718759Exon17: 24 residues, 53719989-53720056Exon18: 88 residues, 53723567-53723827Exon19: 2 residues, -Jump to KGP1A_HUMANExon1: 124 residues, 52504298-52504667Exon2: 57 residues, 52582929-52583096Exon3: 40 residues, 52897488-52897602Exon4: 37 residues, 53234350-53234456Exon5: 23 residues, 53337272-53337336Exon6: 28 residues, 53484249-53484327Exon7: 33 residues, 53492302-53492397Exon8: 24 residues, 53563605-53563671Exon9: 27 residues, 53591654-53591729Exon10: 34 residues, 53681335-53681432Exon11: 48 residues, 53701115-53701255Exon12: 32 residues, 53702157-53702247Exon13: 49 residues, 53710554-53710696Exon14: 56 residues, 53711918-53712082Exon15: 43 residues, 53718491-53718614Exon16: 23 residues, 53718696-53718759Exon17: 24 residues, 53719989-53720056Exon18: 573 residues, 53723567-53725280Exon19: 2 residues, -Jump to KGP1B_HUMAN