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0GRK5_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameGRK5
DescriptionG protein-coupled receptor kinase 5 (ec 2.7.1.-) (g protein-coupled receptor kinase grk5).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005737 cytoplasm (TAS)
0005625 soluble fraction (TAS)
0005543 phospholipid binding (TAS)
0005080 protein kinase C binding (TAS)
0007188 G-protein signaling, coupled to cAMP nucleo... (TAS)
0008277 regulation of G-protein coupled receptor pr... (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
RGS (Regulator of G Protein Signalling) proteins are multi-functional.TPase-accelerating proteins that promote GTP hydrolysis by the alpha subunit of heterotrimeric G proteins.hereby inactivating the G protein and rapidly switching off G protein-coupled receptor signalling pathways . Upon activation by GPCRs.eterotrimeric G proteins exchange GDP for GTP.re released from the receptor.nd dissociate into free.ctive GTP-bound alpha subunit and beta-gamma dimer.oth of which activate downstream effectors. The response is terminated upon GTP hydrolysis by the alpha subunit ().hich can then bind the beta-gamma dimer (. and the receptor. RGS proteins markedly reduce the lifespan of GTP-bound alpha subunits by stabilising the G protein transition state.All RGS proteins contain an RGS-box (or RGS domain).hich is required for activity. Some small RGS proteins such as RGS1 and RGS4 are comprised of little more than an RGS domain.hile others also contain additional domains that confer further functionality . RGS domains can be found in conjunction with a variety of domains.ncluding: DEP for membrane targeting ().DZ for binding to GPCRs ().TB for phosphotyrosine-binding ().BD for Ras-binding ().oLoco for guanine nucleotide inhibitor activity ().X for phosphatidylinositol-binding ().XA that is associated with PX ().H for stimulating guanine nucleotide exchange ().nd GGL (G protein gamma subunit-like) for binding G protein beta subunits () . Those RGS proteins that contain GGL domains can interact with G protein beta subunits to form novel dimers that prevent G protein gamma subunit binding and G protein alpha subunit association.hereby preventing heterotrimer formation.
  IPR000342:Regulator of G protein signalling
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
Rapid regulation of G-protein-coupled receptors (GPCRs) involves agonist-promoted receptor phosphorylation by GPCR kinases (GRKs) . This processis followed by arrestin binding and transient receptor internalisation. It has been shown that beta-adrenergic receptor kinase (beta ARK-1 or GRK2)follows a similar pattern of internalisation upon agonist activation ofbeta(2)-adrenergic receptors (beta(2)AR) and that beta ARK expressionlevels modulate receptor sequestration . Such studies indicate afunctional relationship between receptor phosphorylation and sequestration.howing that beta ARK not only translocates from the cytoplasm to theplasma membrane in response to receptor occupancy.ut also sharesendocytic mechanisms with the beta(2)AR . These results suggest a rolefor beta ARK in the sequestration process.r involvement of receptorinternalisation in the intracellular trafficking of the kinase .
  IPR000239:GPCR kinase
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
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
IPR002290:S_TKc 
Evalue:-83.4436974992327 
Location:186-448IPR000342:RGS 
Evalue:-49.9208183288574 
Location:52-171IPR000961:S_TK_X 
Evalue:-9.01772876696043 
Location:449-528IPR008271:PROTEIN_KINASE_ST 
Evalue:0 
Location:0-0
SequencesProtein: GRK5_HUMAN (590 aa)
mRNA: NM_005308
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
KO assignmentK00924
  Level 3 annotation:
    
  Level 2 annotation:
    Inositol phosphate metabolism
    Nicotinate and nicotinamide metabolism
    Benzoate degradation via CoA ligation
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 96 residues, 120957186-120957471Exon2: 34 residues, 121076017-121076113Exon3: 39 residues, 121130316-121130429Exon4: 28 residues, 121146196-121146274Exon5: 35 residues, 121172667-121172768Exon6: 33 residues, 121174494-121174587Exon7: 23 residues, 121179876-121179940Exon8: 49 residues, 121180888-121181029Exon9: 65 residues, 121186152-121186343Exon10: 14 residues, 121189232-121189270Exon11: 32 residues, 121191500-121191590Exon12: 71 residues, 121193045-121193254Exon13: 48 residues, 121197624-121197762Exon14: 48 residues, 121202172-121202310Exon15: 46 residues, 121202646-121202778Exon16: 218 residues, 121204470-121205120Exon17: 2 residues, -Jump to GRK5_HUMAN  
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