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0MK06_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameMAPK6
DescriptionMitogen-activated protein kinase 6 (ec 2.7.1.37) (extracellular signal-regulated kinase 3) (erk-3) (map kinase isoform p97) (p97- mapk).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0004674 protein serine/threonine kinase activity (TAS)
0006468 protein amino acid phosphorylation (TAS)
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
MAP (Mitogen Activated Protein) kinases participate in kinase cascades.hereby at least 3 protein kinases act in series.ulminating in activationof MAP kinase . MAP kinases are activated by dual phosphorylationon both tyrosine and threonine residues of a conserved TXY motif.ERKs (Extracellularly Regulated Kinases) belong to the family of MAPkinases. ERK 3 and 4.owever.ave no more similarity to ERK 1 and 2 thando the other major classes of MAP kinase.NK and p38. ERK3 isconstitutively located in the nucleus.espite the lack of a traditionalnuclear localisation signal . It is unique among MAP kinases incontaining in its activation loop only a single phosphorylation site (serine189) - other MAP kinases have the sequence TXY in this loop.ut ERK3contains SEG.ith glycine in place of tyrosine.ERK3 has no homologues in nematode or yeast genomes.ndicating that it mayhave arisen from a relatively late gene duplication. Its structure.ased on similarity to ERK2.ontains segregated alpha and beta regions.
  IPR008350:ERK3/4 MAP 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
IPR000719:Pkinase 
Evalue:-88.7695541381836 
Location:20-316
SequencesProtein: MK06_HUMAN (721 aa)
mRNA: NM_002748
Local Annotation
Synapse Ontology
microtubules of the presynaptic compartment function as the tracks for the intense traffic of organelles from cell body to axon terminals and vice versa. It is generally excluded from the presynaptic vesicle cluster.Microtubules do not directly regulate synapse morphology or function
sdb:0087 microtubules  (Evidence:keywords)
KO assignmentK06855
  Level 3 annotation:
    mitogen-activated protein kinase 4/6
  Level 2 annotation:
    MAPK signaling pathway
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 43 residues, 50098738-50098865Exon2: 397 residues, 50125318-50126504Exon3: 50 residues, 50129481-50129626Exon4: 57 residues, 50138121-50138286Exon5: 69 residues, 50140787-50140989Exon6: 789 residues, 50143390-50145751Exon7: 2 residues, -Jump to MK06_HUMAN  
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