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0MAST2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameMAST2
DescriptionMicrotubule-associated serine/threonine-protein kinase 2 (ec 2.7.1.37).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005524 ATP binding (ISS)
0000287 magnesium ion binding (ISS)
0005515 protein binding (IPI)
0006468 protein amino acid phosphorylation (ISS)
0045075 regulation of interleukin-12 biosynthesis (ISS)
0048515 spermatid differentiation (ISS)

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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
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
PDZ domains are found in diverse signaling proteins in bacteria.easts.lants.nsects and vertebrates . PDZ domains can occur in one or multiple copies and are nearly always found in cytoplasmic proteins. They bind either the carboxyl-terminal sequences of proteins or internal peptide sequences . In most cases.nteraction between a PDZ domain and its target is constitutive.ith a binding affinity of 1 to 10 ┬ÁM. However.gonist-dependent activation of cell surface receptors is sometimes required to promote interaction with a PDZ protein. PDZ domain proteins are frequently associated with the plasma membrane. compartment where high concentrations of phosphatidylinositol 4.-bisphosphate (PIP2) are found. Direct interaction between PIP2 and a subset of class II PDZ domains (syntenin.ASK.iam-1) has been demonstrated. PDZ domains consist of 80 to 90 amino acids comprising six beta-strands (betaA to betaF) and two alpha-helices. and B.ompactly arranged in a globular structure. Peptide binding of the ligand takes place in an elongated surface groove as an antiparallel beta-strand interacts with the betaB strand and the B helix. The structure of PDZ domains allows binding to a free carboxylate group at the end of a peptide through a carboxylate-binding loop between the betaA and betaB strands.
  IPR001478:PDZ/DHR/GLGF
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:-98.0655015487564 
Location:512-785IPR001478:PDZ 
Evalue:-12.1135092748275 
Location:1112-1192IPR000961:Pkinase_C 
Evalue:-6.50863838195801 
Location:803-848IPR000719:PROTEIN_KINASE_ATP 
Evalue:0 
Location:0-0
SequencesProtein: MAST2_HUMAN (1798 aa)
mRNA: AB047005 BC065499
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)
activation of protein kinase C
sdb:0206 activation of protein kinase C  (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: 154 residues, 46041871-46042331Exon2: 51 residues, 46062691-46062839Exon3: 49 residues, 46067697-46067840Exon4: 12 residues, 46120622-46120654Exon5: 32 residues, 46197644-46197736Exon6: 27 residues, 46235982-46236058Exon7: 28 residues, 46241063-46241142Exon8: 53 residues, 46244499-46244654Exon9: 27 residues, 46246554-46246630Exon10: 72 residues, 46248988-46249198Exon11: 36 residues, 46257854-46257956Exon12: 46 residues, 46260208-46260341Exon13: 22 residues, 46261168-46261230Exon14: 30 residues, 46261491-46261577Exon15: 71 residues, 46262030-46262239Exon16: 48 residues, 46263935-46264074Exon17: 46 residues, 46265989-46266122Exon18: 57 residues, 46267026-46267192Exon19: 36 residues, 46267724-46267826Exon20: 43 residues, 46268089-46268212Exon21: 38 residues, 46268387-46268497Exon22: 53 residues, 46268865-46269020Exon23: 96 residues, 46269265-46269549Exon24: 67 residues, 46269649-46269844Exon25: 77 residues, 46270436-46270663Exon26: 43 residues, 46270854-46270977Exon27: 47 residues, 46272060-46272197Exon28: 66 residues, 46272331-46272525Exon29: 531 residues, 46272796-46274383Exon30: 2 residues, -Jump to MAST2_HUMANExon1: 145 residues, 46041897-46042331Exon2: 51 residues, 46062691-46062839Exon3: 49 residues, 46067697-46067840Exon4: 12 residues, 46120622-46120654Exon5: 32 residues, 46197644-46197736Exon6: 27 residues, 46235982-46236058Exon7: 28 residues, 46241063-46241142Exon8: 53 residues, 46244499-46244654Exon9: 27 residues, 46246554-46246630Exon10: 72 residues, 46248988-46249198Exon11: 36 residues, 46257854-46257956Exon12: 46 residues, 46260208-46260341Exon13: 22 residues, 46261168-46261230Exon14: 30 residues, 46261491-46261577Exon15: 71 residues, 46262030-46262239Exon16: 48 residues, 46263935-46264074Exon17: 46 residues, 46265989-46266122Exon18: 57 residues, 46267026-46267192Exon19: 36 residues, 46267724-46267826Exon20: 43 residues, 46268089-46268212Exon21: 38 residues, 46268387-46268497Exon22: 53 residues, 46268865-46269020Exon23: 96 residues, 46269265-46269549Exon24: 67 residues, 46269649-46269844Exon25: 77 residues, 46270436-46270663Exon26: 43 residues, 46270854-46270977Exon27: 47 residues, 46272060-46272197Exon28: 65 residues, 46272334-46272525Exon29: 530 residues, 46272796-46274380Exon30: 2 residues, -Jump to MAST2_HUMAN  
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Loci Cluster (Details)Loci: 3799 46426941-46436685 ~-10K 1371(POMGNT1)(-)Loci: 2515 46632578-46652099 ~-20K 1383(FAAH)(+)Loci: 3800 46873299-46906615 ~-33K 1396(-)Loci: 2514 46041871-46274383 ~-233K 1363(MAST2)(+)Link out to UCSC