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0KKCC2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameCAMKK2
DescriptionCalcium/calmodulin-dependent protein kinase kinase 2 (ec 2.7.1.37) (calcium/calmodulin-dependent protein kinase kinase beta) (cam-kinase kinase beta) (cam-kk beta) (camkk beta).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005622 intracellular (ISS)
0005524 ATP binding (NAS)
0005509 calcium ion binding (ISS)
0004685 calcium- and calmodulin-dependent protein k... (NAS)
0005516 calmodulin binding (ISS)
0004674 protein serine/threonine kinase activity (NAS)
0004713 protein-tyrosine kinase activity (ISS)
0046777 autophosphorylation (ISS)
0019722 calcium-mediated signaling (ISS)
0000165 MAPKKK cascade (ISS)
0045941 positive regulation of transcription (ISS)
0045859 regulation of protein kinase activity (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
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:-91.8860566476932 
Location:165-446
SequencesProtein: KKCC2_HUMAN (588 aa)
mRNA: NM_006549
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)
calcium-regulated transcription factor
sdb:0215 calcium-regulated transcription factor  (Evidence:keywords)
KO assignmentK07359
  Level 3 annotation:
    calcium/calmodulin-dependent protein kinase kinase
  Level 2 annotation:
    Adipocytokine signaling pathway
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 1059 residues, 120159879-120163055Exon2: 16 residues, 120166758-120166801Exon3: 35 residues, 120167325-120167426Exon4: 45 residues, 120170791-120170920Exon5: 31 residues, 120171972-120172060Exon6: 26 residues, 120172146-120172220Exon7: 20 residues, 120174846-120174900Exon8: 68 residues, 120175458-120175658Exon9: 31 residues, 120177735-120177824Exon10: 9 residues, 120177968-120177990Exon11: 14 residues, 120182504-120182541Exon12: 46 residues, 120185991-120186125Exon13: 19 residues, 120190823-120190875Exon14: 20 residues, 120191713-120191767Exon15: 18 residues, 120193083-120193131Exon16: 178 residues, 120196241-120196771Exon17: 258 residues, 120219724-120220494Exon18: 2 residues, -Jump to KKCC2_HUMAN  
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Loci Cluster (Details)Loci: 2796 120322284-120346538 ~-24K 9873(RNF34)(+)Loci: 4082 120159879-120220494 ~-61K 9864(CAMKK2)(-)Link out to UCSC