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0MK11_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameMAPK11
DescriptionMitogen-activated protein kinase 11 (ec 2.7.1.37) (mitogen-activated protein kinase p38 beta) (map kinase p38 beta) (p38b) (p38-2) (stress- activated protein kinase 2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0004707 MAP kinase activity (TAS)
0008339 MP kinase activity (IDA)
0019735 antimicrobial humoral response (sensu Verte... (TAS)
0007243 protein kinase cascade (IDA)
0006950 response to stress (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
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.p38 proteins belong to the MAP kinase family and were discovered in 3different contexts independently: first.s tyrosine phosphoproteins foundin extracts of cells treated with inflammatory cytokines; second.stargets of a pyrinidyl imidazole drug that blocks production of TNFalpha; and third.s reactivating kinases for MAP kinase-activated protein(MAPKAP) . The proteins are activated by cytokines.ormones.PCRs.smotic shock.eat shock and other stresses .
  IPR008352:p38 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
IPR002290:S_TKc 
Evalue:-78.267606240177 
Location:24-316IPR008352:P38MAPKINASE 
Evalue:0 
Location:12-21IPR008271:PROTEIN_KINASE_ST 
Evalue:0 
Location:0-0
SequencesProtein: MK11_HUMAN (372 aa)
mRNA: NM_002751
Local Annotation
Synapse Ontology
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
KO assignmentK04441
  Level 3 annotation:
    p38 MAP kinase
  Level 2 annotation:
    MAPK signaling pathway
    Toll-like receptor signaling pathway
    Fc epsilon RI signaling pathway
    Leukocyte transendothelial migration
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 439 residues, 49044269-49045583Exon2: 60 residues, 49045876-49046050Exon3: 28 residues, 49046137-49046216Exon4: 28 residues, 49046781-49046861Exon5: 26 residues, 49047095-49047167Exon6: 40 residues, 49047489-49047604Exon7: 18 residues, 49047682-49047730Exon8: 12 residues, 49047812-49047842Exon9: 39 residues, 49047926-49048038Exon10: 21 residues, 49048124-49048183Exon11: 45 residues, 49048375-49048505Exon12: 60 residues, 49050732-49050906Exon13: 2 residues, -Jump to MK11_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4580 49033457-49042216 ~-9K 25027(MAPK12)(-)Loci: 4581 49044269-49050906 ~-7K 25029(MAPK11)(-)Loci: 4582 49308864-49310838 ~-2K 25050(SCO2)(-)Loci: 4583 49311049-49315321 ~-4K 25051(ECGF1)(-)Loci: 4584 49354156-49363744 ~-10K 25054(CPT1B)(-)Loci: 4579 48998244-49025527 ~-27K 25025(TUBGCP6)(-)Link out to UCSC