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1Q9BUB1_HUMAN*   Trembl (?) | Description Local Annotation Link Reference
General Information
NameN/A
DescriptionPrkar2a protein (protein kinase, camp-dependent, regulatory, type ii, alpha).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005952 cAMP-dependent protein kinase complex (IEA)
0008603 cAMP-dependent protein kinase regulator act... (IEA)
0016301 kinase activity (IEA)
0006468 protein amino acid phosphorylation (IEA)
0007165 signal transduction (IEA)

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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:
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. This family of RII alpha.he regulatory subunit portion of type II PKA proteins.ontains the dimerisation interface and binding site for A-kinase-anchoring proteins (AKAPs).
  IPR003117:cAMP-dependent protein kinase regulator, type II PKA R subunit
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
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
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. Typical R subunits have a conserved domain structure.onsisting of the N-terminal dimerisation 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.On the basis of phylogenetic trees generated from multiple sequence alignment of complete sequences.his family was divided into four sub-families.ypes I to IV . Types I and II.ound in animals.iffer in molecular weight.equence.utophosphorylation capability.ellular location and tissue distribution. Types I and II are further sub-divided into alpha and beta subtypes.ased mainly on sequence similarity. Type III are from fungi and type IV are from alveolates.
  IPR012198:cAMP-dependent protein kinase regulatory subunit
IPR000595:cNMP 
Evalue:-24.2757241303992 
Location:139-259IPR003117:RIIa 
Evalue:-17.7447280883789 
Location:8-45IPR000595:cNMP_binding 
Evalue:-8.95860767364502 
Location:279-354
SequencesProtein: Q9BUB1_HUMAN (382 aa)
mRNA: BC002763
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 assignmentK04739
  Level 3 annotation:
    cAMP-dependent protein kinase regulator
  Level 2 annotation:
    Insulin signaling pathway
    Apoptosis
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 686 residues, 48762098-48764155Exon2: 49 residues, 48764612-48764754Exon3: 27 residues, 48777440-48777515Exon4: 36 residues, 48777684-48777786Exon5: 53 residues, 48785391-48785545Exon6: 37 residues, 48795422-48795529Exon7: 30 residues, 48802980-48803064Exon8: 19 residues, 48806433-48806486Exon9: 14 residues, 48820085-48820121Exon10: 166 residues, 48859771-48860265Exon11: 2 residues, -Jump to Q9BUB1_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4601 48530128-48569231 ~-39K 25651(PFKFB4)(-)Loci: 4602 48611435-48622102 ~-11K 25656(UQCRC1)(-)Loci: 4603 48637834-48684985 ~-47K 25658(CELSR3)(-)Loci: 4604 48686283-48698338 ~-12K 25669(NCKIPSD)(-)Loci: 4605 48762098-48860265 ~-98K 25672(-)Loci: 4606 49133551-49145603 ~-12K 25699(LAMB2)(-)Loci: 4607 49429215-49435016 ~-6K 25713(AMT)(-)Loci: 3354 49566925-49683976 ~-117K 25718(BSN)(+)Loci: 4608 49921309-49942261 ~-21K 25739(-)Loci: 4609 50330243-50333903 ~-4K 25774(HYAL2)(-)Loci: 4600 48420266-48441746 ~-21K 25634(PLXNB1)(-)Link out to UCSC