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0STK4_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSTK4
DescriptionSerine/threonine-protein kinase 4 (ec 2.7.1.37) (ste20-like kinase mst1) (mst-1) (mammalian ste20-like protein kinase 1) (serine/threonine-protein kinase krs-2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005524 ATP binding (IDA)
0000287 magnesium ion binding (IDA)
0046983 protein dimerization activity (IDA)
0042802 protein self binding (IPI)
0004674 protein serine/threonine kinase activity (IDA)
0043065 positive regulation of apoptosis (IDA)
0006468 protein amino acid phosphorylation (IDA)
0007243 protein kinase cascade (IDA)
0007165 signal transduction (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
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:-103.376750709602 
Location:30-281IPR011524:SARAH 
Evalue:0 
Location:433-480IPR008271:PROTEIN_KINASE_ST 
Evalue:0 
Location:0-0
SequencesProtein: STK4_HUMAN (487 aa)
mRNA: NM_006282
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)
KO assignmentK04411
  Level 3 annotation:
    serine/threonine kinase 4
  Level 2 annotation:
    MAPK signaling pathway
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 42 residues, 43028533-43028658Exon2: 29 residues, 43034132-43034213Exon3: 45 residues, 43040497-43040626Exon4: 40 residues, 43043883-43043998Exon5: 57 residues, 43049186-43049351Exon6: 58 residues, 43057144-43057312Exon7: 48 residues, 43059223-43059361Exon8: 45 residues, 43062446-43062575Exon9: 64 residues, 43063221-43063408Exon10: 54 residues, 43087027-43087185Exon11: 1646 residues, 43137072-43142005Exon12: 2 residues, -Jump to STK4_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3258 42947757-42970574 ~-23K 23159(YWHAB)(+)Loci: 3259 43028533-43142005 ~-113K 23166(STK4)(+)Loci: 4524 43154364-43163167 ~-9K 23170(KCNS1)(-)Loci: 3260 43478191-43488296 ~-10K 23191(PIGT)(+)Loci: 4523 42813862-42872326 ~-58K 23158(RIMS4)(-)Link out to UCSC