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0MLTK_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameMLTK
DescriptionMitogen-activated protein kinase kinase kinase mlt (ec 2.7.1.37) (mlk- like mitogen-activated protein triple kinase) (leucine zipper and sterile alpha motif kinase zak) (sterile-alpha motif and leucine zipper containing kinase azk) (mixed lineage kinase-related kinase mrk) (cervical cancer suppressor gene 4 protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005737 cytoplasm (ISS)
0005524 ATP binding (IDA)
0000287 magnesium ion binding (IDA)
0042802 protein self binding (IPI)
0004674 protein serine/threonine kinase activity (IDA)
0000075 cell cycle checkpoint (IDA)
0043065 positive regulation of apoptosis (IDA)
0006468 protein amino acid phosphorylation (IDA)
0007243 protein kinase cascade (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:
Protein kinases comprise a large family of enzymes that mediate the response of eukaryotic cells to external stimuli by phosphorylation of hydroxyamino acids. The enzymes fall into two broad classes.haracterised with respect to substrate specificity: serine/threonine specific and tyrosine specific . Tyrosine phosphorylating activity was originally detected in two viral transforming proteins .ut many retroviral transforming proteins and their cellular counterparts have since been shown to possess such activity. The growth factor receptors.hich are activated by ligand binding.nd theinsulin-related peptide receptor.re also family members.
  IPR001245:Tyrosine protein kinase
This entry represents a second domain related to the SAM domain. Sterile alpha motif (SAM) domains are known to be involved in diverse protein-protein interactions.ssociating with both SAM-containing and non-SAM-containing protein pathways.
  IPR011510:Sterile alpha motif homology 2
The sterile alpha motif (SAM) domain is a putative protein interaction module present in a wide variety of proteins involved in many biological processes. The SAM domain that spreads over around 70 residues is found in diverse eukaryotic organisms . SAM domains have been shown to homo- and hetero-oligomerise.orming multiple self-association architectures and also binding to various non-SAM domain-containing proteins .evertheless with a low affinity constant . SAM domains also appear to possess the ability to bind RNA . Smaug a protein that helps to establish a morphogen gradient in Drosophila embryos by repressing the translation of nanos (nos) mRNA binds to the 3 untranslated region (UTR) of nos mRNA via two similar hairpin structures. The 3D crystal structure of the Smaug RNA-binding region shows a cluster of positively charged residues on the Smaug-SAM domain.hich could be the RNA-binding surface. This electropositive potential is unique among all previously determined SAM-domain structures and is conserved among Smaug-SAM homologs. These results suggest that the SAM domain might have a primary role in RNA binding. Structural analyses show that the SAM domain is arranged in a small five-helix bundle with two large interfaces . In the case of the SAM domain of EphB2.ach of these interfaces is able to form dimers. The presence of these two distinct intermonomers binding surface suggest that SAM could form extended polymeric structures .
  IPR001660:Sterile alpha motif SAM
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
Sterile alpha motif (SAM) domains are known to be involved in diverse protein-protein interactions.ssociating with both SAM-containing and non-SAM-containing proteins pathway . SAM domains exhibit a conserved structure.onsisting of a 4-5-helical bundle of two orthogonally packed alpha-hairpins. However SAM domains display a diversity of function.eing involved in interactions with proteins.NA and RNA . The name sterile alpha motif arose from its presence in proteins that are essential for yeast sexual differentiation. The SAM domain has had various names.ncluding SPM.TN (pointed).EP (yeast sterility.ts-related.cG proteins).CR (N-terminal conserved region) and HLH (helix-loop-helix) domain.ll of which are related and can be classified as SAM domains. SAM domains occur in eukaryotic and in some bacterial proteins. Structures have been determined for several proteins that contain SAM domains.ncluding Ets-1 transcription factor.hich plays a role in the development and invasion of tumour cells by regulating the expression of matrix-degrading proteases ; Etv6 transcription factor.ene rearrangements of which have been demonstrated in several malignancies ; EphA4 receptor tyrosine kinase.hich is believed to be important for the correct localization of a motoneuron pool to a specific position in the spinal cord ; EphB2 receptor.hich is involved in spine morphogenesis via intersectin.dc42 and N-Wasp ; p73. p53 homologue involved in neuronal development ; and polyhomeotic.hich is a member of the Polycomb group of genes (Pc-G) required for the maintenance of the spatial expression pattern of homeotic genes .
  IPR013761:Sterile alpha motif-type
IPR001245:Pkinase_Tyr 
Evalue:-68.7958831787109 
Location:16-260IPR011510:SAM_2 
Evalue:-8.65757751464844 
Location:361-410IPR000719:PROTEIN_KINASE_ATP 
Evalue:0 
Location:0-0
SequencesProtein: MLTK_HUMAN (800 aa)
mRNA: NM_016653
Local Annotation
Synapse Ontology
A process that increases short-term neuronal synaptic plasticity, the ability of neuronal synapses to change in the short-term as circumstances require. Short-term neuronal synaptic plasticity generally involves increasing or decreasing synaptic sensitivity.
sdb:0043 positive regulation of short-term neuronal synaptic plasticity  (Evidence:keywords)
the plasma membrane of the postsynaptic neuron. It apposes with presynaptic actiove zone.
sdb:0108 postsynaptic plasma membrane  (Evidence:keywords)
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
KO assignmentK04424
  Level 3 annotation:
    sterile alpha motif and leucine zipper containing kinase AZK
  Level 2 annotation:
    MAPK signaling pathway
    Tight junction
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 56 residues, 173648810-173648976Exon2: 66 residues, 173663971-173664164Exon3: 31 residues, 173742778-173742866Exon4: 36 residues, 173755827-173755929Exon5: 24 residues, 173760531-173760597Exon6: 11 residues, 173763868-173763897Exon7: 48 residues, 173764013-173764151Exon8: 31 residues, 173770999-173771086Exon9: 27 residues, 173776769-173776844Exon10: 37 residues, 173782702-173782809Exon11: 47 residues, 173790088-173790224Exon12: 17 residues, 173802662-173802707Exon13: 12 residues, 173805165-173805196Exon14: 48 residues, 173805293-173805433Exon15: 23 residues, 173811346-173811409Exon16: 33 residues, 173812377-173812470Exon17: 41 residues, 173831672-173831789Exon18: 27 residues, 173834036-173834111Exon19: 52 residues, 173836718-173836869Exon20: 655 residues, 173839023-173840982Exon21: 2 residues, -Jump to MLTK_HUMAN  
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