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0ST38L_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSTK38L
DescriptionSerine/threonine-protein kinase 38-like (ec 2.7.1.37) (ndr2 protein kinase) (nuclear dbf2-related kinase 2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0015629 actin cytoskeleton (ISS)
0005737 cytoplasm (IDA)
0005524 ATP binding (IDA)
0000287 magnesium ion binding (IDA)
0004674 protein serine/threonine kinase activity (IDA)
0006468 protein amino acid phosphorylation (IDA)
0007243 protein kinase cascade (IDA)
0051128 regulation of cell organization and biogenesis (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 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
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:-99.9586073148418 
Location:90-383IPR000961:Pkinase_C 
Evalue:-10.4948501586914 
Location:401-447
SequencesProtein: ST38L_HUMAN (464 aa)
mRNA: NM_015000
Local Annotation
Synapse Ontology
activation of protein kinase C
sdb:0206 activation of protein kinase C  (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: 53 residues, 27288374-27288532Exon2: 50 residues, 27341909-27342054Exon3: 19 residues, 27346336-27346388Exon4: 43 residues, 27352538-27352661Exon5: 30 residues, 27353313-27353397Exon6: 43 residues, 27356748-27356872Exon7: 53 residues, 27358703-27358858Exon8: 36 residues, 27359214-27359317Exon9: 22 residues, 27359488-27359550Exon10: 41 residues, 27361535-27361653Exon11: 43 residues, 27362095-27362219Exon12: 34 residues, 27363527-27363623Exon13: 32 residues, 27366342-27366434Exon14: 1091 residues, 27366527-27369794Exon15: 2 residues, -Jump to ST38L_HUMAN  
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