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0MASTL_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameMASTL
DescriptionMicrotubule-associated serine/threonine-protein kinase-like (ec 2.7.1.37).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
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
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
IPR000719:Pkinase 
Evalue:-43.3279037475586 
Location:35-183IPR000719:Pkinase 
Evalue:-26.3010292053223 
Location:740-835IPR000961:S_TK_X 
Evalue:-0.721246399047171 
Location:836-876IPR000719:PROTEIN_KINASE_ATP 
Evalue:0 
Location:0-0
SequencesProtein: MASTL_HUMAN (879 aa)
mRNA: BC009107 NM_032844
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
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 assignmentK00870
  Level 3 annotation:
    protein kinase
  Level 2 annotation:
    Signal transduction mechanisms
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 84 residues, 27484297-27484547Exon2: 48 residues, 27487483-27487621Exon3: 48 residues, 27488553-27488693Exon4: 31 residues, 27490028-27490117Exon5: 37 residues, 27493998-27494105Exon6: 52 residues, 27494323-27494474Exon7: 59 residues, 27496036-27496209Exon8: 382 residues, 27498878-27500018Exon9: 48 residues, 27502055-27502194Exon10: 40 residues, 27509887-27510001Exon11: 36 residues, 27510414-27510516Exon12: 182 residues, 27515313-27515854Exon13: 2 residues, -Jump to MASTL_HUMANExon1: 82 residues, 27484304-27484547Exon2: 48 residues, 27487483-27487621Exon3: 48 residues, 27488553-27488693Exon4: 31 residues, 27490028-27490117Exon5: 37 residues, 27493998-27494105Exon6: 52 residues, 27494323-27494474Exon7: 59 residues, 27496036-27496209Exon8: 382 residues, 27498878-27500018Exon9: 49 residues, 27502052-27502194Exon10: 40 residues, 27509887-27510001Exon11: 36 residues, 27510414-27510516Exon12: 150 residues, 27515313-27515759Exon13: 2 residues, -Jump to MASTL_HUMAN  
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Loci Cluster (Details)Loci: 3882 27439390-27483327 ~-44K 4619(YME1L1)(-)Loci: 2608 27484297-27515854 ~-32K 4624(MASTL)(+)Loci: 2609 27833220-27869103 ~-36K 4631(RAB18)(+)Loci: 3881 27075532-27189965 ~-114K 4610(ABI1)(-)Link out to UCSC