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0DCAK1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameDCAMKL1
DescriptionSerine/threonine-protein kinase dcamkl1 (ec 2.7.1.37) (doublecortin- like and cam kinase-like 1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005887 integral to plasma membrane (TAS)
0005515 protein binding (NAS)
0004672 protein kinase activity (TAS)
0005057 receptor signaling protein activity (TAS)
0007417 central nervous system development (TAS)
0016197 endosome transport (NAS)
0006468 protein amino acid phosphorylation (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
X-linked lissencephaly is a severe brain malformation affecting males.Recently it has been demonstrated that the doublecortin gene is implicated inthis disorder . Doublecortin was found to bind to the microtubulecytoskeleton. In vivo and in vitro assays show that Doublecortin stabilizesmicrotubules and causes bundling . Doublecortin is a basic protein with aniso-electric point of 10.ypical of microtubule-binding proteins. However.ts sequence contains no known microtubule-binding domain(s). The detailed sequence analysis of Doublecortin and Doublecortin-like proteinsallowed the identification of an evolutionarily conserved Doublecortin (DC)domain. This domain is found in the N-terminus of proteins and consists of oneor two tandemly repeated copies of an around 80 amino acids region. It hasbeen suggested that the first DC domain of Doublecortin binds tubulin andenhances microtubule polymerization .
  IPR003533:Doublecortin
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:-103.657577319178 
Location:390-647IPR003533:DCX 
Evalue:-42.7958800173441 
Location:52-143IPR003533:DCX 
Evalue:-34.602059991328 
Location:181-269
SequencesProtein: DCAK1_HUMAN (740 aa)
mRNA: NM_004734
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (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)
KO assignmentK00870
  Level 3 annotation:
    protein kinase
  Level 2 annotation:
    Signal transduction mechanisms
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 1120 residues, 35243477-35246836Exon2: 26 residues, 35260348-35260422Exon3: 40 residues, 35265502-35265616Exon4: 29 residues, 35277835-35277916Exon5: 34 residues, 35280360-35280457Exon6: 28 residues, 35281154-35281232Exon7: 46 residues, 35282971-35283105Exon8: 51 residues, 35294865-35295012Exon9: 42 residues, 35299771-35299891Exon10: 21 residues, 35300386-35300444Exon11: 38 residues, 35308169-35308278Exon12: 30 residues, 35311228-35311313Exon13: 33 residues, 35326635-35326730Exon14: 41 residues, 35343360-35343477Exon15: 35 residues, 35419494-35419594Exon16: 117 residues, 35584005-35584352Exon17: 133 residues, 35597898-35598293Exon18: 66 residues, 35603250-35603443Exon19: 2 residues, -Jump to DCAK1_HUMAN  
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