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0KPCD2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePRKD2
DescriptionProtein kinase c, d2 type (ec 2.7.1.-) (npkc-d2) (protein kinase d2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005622 intracellular (NAS)
0005524 ATP binding (NAS)
0004674 protein serine/threonine kinase activity (NAS)
0007242 intracellular signaling cascade (NAS)
0006468 protein amino acid phosphorylation (NAS)

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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
Diacylglycerol (DAG) is an important second messenger. Phorbol esters (PE) are analogues of DAG and potent tumor promoters that cause a variety of physiological changes when administered to both cells and tissues. DAG activates a family of serine/threonine protein kinases.ollectively known as protein kinase C (PKC) . Phorbol esters can directly stimulate PKC. The N-terminal region of PKC.nown as C1.as been shown to bind PE and DAG in a phospholipid and zinc-dependent fashion. The C1 region contains one or two copies (depending on the isozyme of PKC) of a cysteine-rich domain.hich is about 50 amino-acid residues long.nd which is essential for DAG/PE-binding. The DAG/PE-binding domain binds two zinc ions; the ligands of these metal ions are probably the six cysteines and two histidines that are conserved in this domain.
  IPR002219:Protein kinase C, phorbol ester/diacylglycerol binding
The pleckstrin homology (PH) domain is a domain of about 100 residues that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton .The function of this domain is not clear.everal putative functions have been suggested:binding to the beta/gamma subunit of heterotrimeric G proteins.inding to lipids..g. phosphatidylinositol-4.-bisphosphate.inding to phosphorylated Ser/Thr residues.ttachment to membranes by an unknown mechanism.It is possible that different PH domains have totally different ligand requirements.The 3D structure of several PH domains has been determined . All known cases have a common structure consisting of two perpendicular anti-parallel beta sheets.ollowed by a C-terminal amphipathic helix. The loops connecting the beta-strands differ greatly in length.aking the PH domain relatively difficult to detect. There are no totally invariant residues within the PH domain.Proteins reported to contain one more PH domains belong to the following families:Pleckstrin.he protein where this domain was first detected.s the major substrate of protein kinase C in platelets. Pleckstrin is one of the rare proteins to contains two PH domains.Ser/Thr protein kinases such as the Akt/Rac family.he beta-adrenergic receptor kinases.he mu isoform of PKC and the trypanosomal NrkA family.Tyrosine protein kinases belonging to the Btk/Itk/Tec subfamily.Insulin Receptor Substrate 1 (IRS-1).Regulators of small G-proteins like guanine nucleotide releasing factor GNRP (Ras-GRF) (which contains 2 PH domains).uanine nucleotide exchange proteins like vav.bl.oS and Saccharomyces cerevisiae CDC24.TPase activating proteins like rasGAP and BEM2/IPL2.nd the human break point cluster protein bcr.Cytoskeletal proteins such as dynamin (see ).aenorhabditis elegans kinesin-like protein unc-104 (see ).pectrin beta-chain.yntrophin (2 PH domains) and S. cerevisiae nuclear migration protein NUM1.Mammalian phosphatidylinositol-specific phospholipase C (PI-PLC) (see ) isoforms gamma and delta. Isoform gamma contains two PH domains.he second one is split into two parts separated by about 400 residues.Oxysterol binding proteins OSBP.. cerevisiae OSH1 and YHR073w.Mouse protein citron. putative rho/rac effector that binds to the GTP-bound forms of rho and rac.Several S. cerevisiae proteins involved in cell cycle regulation and bud formation like BEM2.EM3.UD4 and the BEM1-binding proteins BOI2 (BEB1) and BOI1 (BOB1).C. elegans protein MIG-10.C. elegans hypothetical proteins C04D8.1.06H7.4 and ZK632.12.S. cerevisiae hypothetical proteins YBR129c and YHR155w.
  IPR001849:Pleckstrin-like
Pleckstrin homology (PH) domains are small modular domains that occur once.r occasionally several times.n a large variety of signalling proteins.here they serve as simple targeting domains that recognize only phosphoinositide headgroups . PH domains can target their host protein to the plasma and internal membranes through its association with phosphoinositides. PH domains have a partly opened beta-barrel topology that is capped by an alpha helix. Proteins containing PH domains include pleckstrin (N-terminal).hospholipase C delta-1.eta-spectrin.ynamin.on-of-sevenless.rp1.nc-89.app1 and Rac-alpha kinase.The structure of PH domains is similar to the phosphotyrosine-binding domain (PTB) found in IRS-1 (insulin receptor substrate 1).hc adaptor and Numb; to the Ran-binding domain.ound in Nup nuclear pore complex and Ranbp1; to the Enabled/VASP homology domain 1 (EVH1 domain).ound in Enabled.ASP (vasodilator-stimulated phosphoprotein).omer and WASP actin regulatory protein; to the third domain of FERM.ound in moesin.adixin.zrin.erlin and talin; and to the PH-like domain of neurobeachin.
  IPR011993:Pleckstrin homology-type
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:-90.8860566476932 
Location:551-807IPR002219:C1_1 
Evalue:-17.408935546875 
Location:265-317IPR002219:C1_1 
Evalue:-16.0915145874023 
Location:139-191IPR001849:PH 
Evalue:-9.13667678833008 
Location:398-478
SequencesProtein: KPCD2_HUMAN (878 aa)
mRNA: NM_016457
Local Annotation
Synapse Ontology
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
KO assignmentK06070
  Level 3 annotation:
    protein kinase D
  Level 2 annotation:
    Signal transduction mechanisms
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 140 residues, 51869413-51869832Exon2: 30 residues, 51870129-51870215Exon3: 91 residues, 51873492-51873760Exon4: 35 residues, 51876746-51876845Exon5: 56 residues, 51884633-51884795Exon6: 37 residues, 51885696-51885803Exon7: 26 residues, 51886831-51886904Exon8: 19 residues, 51887029-51887082Exon9: 88 residues, 51888971-51889230Exon10: 28 residues, 51892253-51892331Exon11: 41 residues, 51892829-51892947Exon12: 53 residues, 51895895-51896049Exon13: 28 residues, 51896131-51896209Exon14: 76 residues, 51899265-51899488Exon15: 53 residues, 51899591-51899746Exon16: 46 residues, 51906003-51906135Exon17: 48 residues, 51908959-51909098Exon18: 95 residues, 51911227-51911506Exon19: 2 residues, -Jump to KPCD2_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3116 50100878-50104489 ~-4K 19057(APOE)(+)Loci: 3117 50234137-50266053 ~-32K 19065(SFRS16)(+)Loci: 4398 50407718-50429309 ~-22K 19076(-)Loci: 3118 50446389-50500381 ~-54K 19078(MARK4)(+)Loci: 4399 50546685-50565669 ~-19K 19089(ERCC2)(-)Loci: 4400 50747641-50779917 ~-32K 19109(OPA3)(-)Loci: 4401 50804499-50834509 ~-30K 19111(EML2)(-)Loci: 3119 50863341-50877557 ~-14K 19113(GIPR)(+)Loci: 4402 51134630-51168497 ~-34K 19134(NOVA2)(-)Loci: 3120 51542133-51585943 ~-44K 19149(PPP5C)(+)Loci: 3121 51796351-51805878 ~-10K 19157(CALM1)(+)Loci: 4403 51869413-51911506 ~-42K 19161(PRKD2)(-)Loci: 4404 52033262-52046043 ~-13K 19167(AP2S1)(-)Loci: 3115 50004177-50016517 ~-12K 19053(LU)(+)Link out to UCSC