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0KPCI_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePRKCI
DescriptionProtein kinase c, iota type (ec 2.7.1.37) (npkc-iota) (atypical protein kinase c-lambda/iota) (apkc-lambda/iota) (prkc-lambda/iota).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005829 cytosol (ISS)
0005634 nucleus (ISS)
0000133 polarisome (ISS)
0005524 ATP binding (ISS)
0004700 atypical protein kinase C activity (ISS)
0005543 phospholipid binding (ISS)
0005515 protein binding (IPI)
0007010 cytoskeleton organization and biogenesis (ISS)
0045197 establishment and/or maintenance of epithel... (ISS)
0045216 intercellular junction assembly and/or main... (ISS)
0016044 membrane organization and biogenesis (ISS)
0006468 protein amino acid phosphorylation (TAS)
0006612 protein-membrane targeting (ISS)
0046903 secretion (ISS)
0007165 signal transduction (TAS)
0016192 vesicle-mediated transport (ISS)

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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 Phox and Bem1p domain.s present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold.imilar tothat found in ubiquitin and Ras-binding domains. A motif.ariously termed OPR.C and AID.epresents the most conserved region of the majority of PB1 domains.nd is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers.lthough not all PB1 domain pairs associate.
  IPR000270:Octicosapeptide/Phox/Bem1p
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
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
This group represents a protein kinase C.eta/iota types. Please see the following relevant reference: .
  IPR012233:Protein kinase C, zeta/iota
IPR002290:S_TKc 
Evalue:-95.3665315444204 
Location:245-513IPR000270:PB1 
Evalue:-24.1366771398795 
Location:16-97IPR002219:C1_1 
Evalue:-20.4202156066895 
Location:132-184IPR000961:S_TK_X 
Evalue:-19.4559319556497 
Location:514-577
SequencesProtein: KPCI_HUMAN (587 aa)
mRNA: BC022016 NM_002740
Local Annotation
Synapse Ontology
The assembly and arrangement of the membrane surrounding a synaptic vesicle.
sdb:0073 synaptic vesicle membrane organization and biogenesis  (Evidence:keywords)
endosome of the presynaptic compartment. A cellular structure that is involved in the transport of proteins in the neuron after the proteins are endocytosed from the outside to the inside of the cell.
sdb:0088 endosome  (Evidence:keywords)
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
Some have one process that touches a blood vessel while other processes touch neurons-- this is thought to aid neurons in obtaining nutrients; the processes of the astrocytes that touch the blood vessels are called astrocytic endfeet. Satellite cells, one kind of glias in PNS, are supportive cells in the PNS, found near PNS neuronal cell bodies.
sdb:0225 provide nutrition and maintenance of structure  (Evidence:keywords)
?
sdb:0247 cytoskeleton protein transport  (Evidence:keywords)
KO assignmentK06069
  Level 3 annotation:
    atypical protein kinase C
  Level 2 annotation:
    Insulin signaling pathway
    Tight junction
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 112 residues, 171422918-171423252Exon2: 42 residues, 171435711-171435833Exon3: 32 residues, 171460450-171460540Exon4: 19 residues, 171463860-171463911Exon5: 30 residues, 171468396-171468482Exon6: 49 residues, 171470902-171471043Exon7: 20 residues, 171473767-171473822Exon8: 21 residues, 171475710-171475769Exon9: 61 residues, 171480708-171480885Exon10: 34 residues, 171481647-171481745Exon11: 31 residues, 171482363-171482450Exon12: 47 residues, 171484942-171485078Exon13: 31 residues, 171492335-171492423Exon14: 44 residues, 171493864-171493990Exon15: 28 residues, 171496392-171496472Exon16: 32 residues, 171497785-171497875Exon17: 40 residues, 171499476-171499592Exon18: 981 residues, 171503521-171506458Exon19: 2 residues, -Jump to KPCI_HUMANExon1: 111 residues, 171422920-171423252Exon2: 42 residues, 171435711-171435833Exon3: 32 residues, 171460450-171460540Exon4: 19 residues, 171463860-171463911Exon5: 30 residues, 171468396-171468482Exon6: 49 residues, 171470902-171471043Exon7: 20 residues, 171473767-171473822Exon8: 21 residues, 171475710-171475769Exon9: 61 residues, 171480708-171480885Exon10: 34 residues, 171481647-171481745Exon11: 31 residues, 171482363-171482450Exon12: 47 residues, 171484942-171485078Exon13: 31 residues, 171492335-171492423Exon14: 44 residues, 171493864-171493990Exon15: 28 residues, 171496392-171496472Exon16: 32 residues, 171497785-171497875Exon17: 40 residues, 171499476-171499592Exon18: 124 residues, 171503521-171503889Exon19: 2 residues, -Jump to KPCI_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3383 171619358-171634577 ~-15K 26820(CLDN11)(+)Loci: 3382 171422918-171506458 ~-84K 26816(PRKCI)(+)Link out to UCSC