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0MKNK2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameMKNK2
DescriptionMap kinase-interacting serine/threonine-protein kinase 2 (ec 2.7.1.37) (map kinase signal-integrating kinase 2) (mnk2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005524 ATP binding (IDA)
0004674 protein serine/threonine kinase activity (IDA)
0007166 cell surface receptor linked signal transdu... (TAS)
0006468 protein amino acid phosphorylation (IDA)
0007243 protein kinase cascade (IDA)
0006445 regulation of translation (IDA)

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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:-87.1366771398795 
Location:83-368
SequencesProtein: MKNK2_HUMAN (418 aa)
mRNA: AF237775 NM_199054
Local Annotation
Synapse Ontology
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
KO assignmentK04372
  Level 3 annotation:
    mitogen and stress response kinase
  Level 2 annotation:
    MAPK signaling pathway
    Insulin signaling pathway
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 796 residues, 1988469-1990855Exon2: 16 residues, 1991132-1991176Exon3: 57 residues, 1992038-1992203Exon4: 67 residues, 1992838-1993033Exon5: 34 residues, 1993425-1993521Exon6: 20 residues, 1993605-1993661Exon7: 37 residues, 1993764-1993869Exon8: 26 residues, 1994122-1994196Exon9: 28 residues, 1994501-1994581Exon10: 34 residues, 1997184-1997282Exon11: 36 residues, 1997365-1997467Exon12: 31 residues, 1997602-1997690Exon13: 51 residues, 2001799-2001946Exon14: 48 residues, 2002094-2002233Exon15: 2 residues, -Jump to MKNK2_HUMANExon1: 85 residues, 1990601-1990855Exon2: 16 residues, 1991132-1991176Exon3: 57 residues, 1992038-1992203Exon4: 67 residues, 1992838-1993033Exon5: 34 residues, 1993425-1993521Exon6: 20 residues, 1993605-1993661Exon7: 37 residues, 1993764-1993869Exon8: 26 residues, 1994122-1994196Exon9: 28 residues, 1994501-1994581Exon10: 34 residues, 1997184-1997282Exon11: 36 residues, 1997365-1997467Exon12: 31 residues, 1997602-1997690Exon13: 31 residues, 2001799-2001886Exon14: 2 residues, -Jump to MKNK2_HUMAN  
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Loci Cluster (Details)Loci: 4349 568224-584530 ~-16K 17494(POLRMT)(-)Loci: 3077 868357-872013 ~-4K 17519(GPR54)(+)Loci: 3078 951436-960723 ~-9K 17523(GRIN3B)(+)Loci: 3079 1192748-1195823 ~-3K 17537(ATP5D)(+)Loci: 3080 1334888-1346583 ~-12K 17550(+)Loci: 4350 1766247-1799450 ~-33K 17579(-)Loci: 4351 1988469-2002233 ~-14K 17594(MKNK2)(-)Loci: 4352 2051987-2102554 ~-51K 17601(AP3D1)(-)Loci: 3076 540892-568157 ~-27K 17493(HCN2)(+)Link out to UCSC