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0MARK4_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameMARK4
DescriptionMap/microtubule affinity-regulating kinase 4 (ec 2.7.1.37) (map/microtubule affinity-regulating kinase-like 1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005813 centrosome (IDA)
0015630 microtubule cytoskeleton (IDA)
0043005 neuron projection (IDA)
0005524 ATP binding (NAS)
0043015 gamma-tubulin binding (IDA)
0008017 microtubule binding (IDA)
0004674 protein serine/threonine kinase activity (IDA)
0050321 tau-protein kinase activity (IDA)
0043130 ubiquitin binding (NAS)
0001578 microtubule bundle formation (IEP)
0007399 neurogenesis (IDA)
0043068 positive regulation of programmed cell death (NAS)
0006468 protein amino acid phosphorylation (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 domain is found in the C-terminal extremity of various serine/threonine-protein kinases from fungi.lants and animals.
  IPR001772:Kinase-associated, C-terminal
UBA domains are a commonly occurring sequence motif of approximately 45 amino acid residues that are found in diverse proteins involved in the ubiquitin/proteasome pathway.NA excision-repair.nd cell signaling via protein kinases . The human homologue of yeast Rad23A is one example of a nucleotide excision-repair protein that contains both an internal and a C-terminal UBA domain. The solution structure of human Rad23A UBA(2) showed that the domain forms a compact three-helix bundle . Comparison of the structures of UBA(1) and UBA(2) reveals that both form very similar folds and have a conserved large hydrophobic surface patch which may be a common protein-interacting surface present in diverse UBA domains. Evidence that ubiquitin binds to UBA domains leads to the prediction that the hydrophobic surface patch of UBA domains interacts with the hydrophobic surface on the five-stranded beta-sheet of ubiquitin .
  IPR000449:Ubiquitin-associated
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:-108.853871964322 
Location:59-310IPR001772:KA1 
Evalue:-10.958607673645 
Location:703-752IPR000449:UBA 
Evalue:-6.32790214206428 
Location:331-368
SequencesProtein: MARK4_HUMAN (752 aa)
mRNA: AB088047 NM_031417
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)
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: 117 residues, 50446389-50446737Exon2: 69 residues, 50454086-50454287Exon3: 20 residues, 50458210-50458264Exon4: 18 residues, 50458416-50458465Exon5: 24 residues, 50459781-50459847Exon6: 25 residues, 50459937-50460008Exon7: 21 residues, 50461322-50461379Exon8: 81 residues, 50466569-50466806Exon9: 42 residues, 50473020-50473140Exon10: 35 residues, 50473613-50473713Exon11: 38 residues, 50475471-50475581Exon12: 55 residues, 50475672-50475832Exon13: 74 residues, 50482544-50482762Exon14: 36 residues, 50489446-50489550Exon15: 95 residues, 50492773-50493052Exon16: 17 residues, 50494908-50494953Exon17: 438 residues, 50497471-50498779Exon18: 2 residues, -Jump to MARK4_HUMANExon1: 19 residues, 50446681-50446737Exon2: 69 residues, 50454086-50454287Exon3: 20 residues, 50458210-50458264Exon4: 18 residues, 50458416-50458465Exon5: 24 residues, 50459781-50459847Exon6: 25 residues, 50459937-50460008Exon7: 21 residues, 50461322-50461379Exon8: 81 residues, 50466569-50466806Exon9: 42 residues, 50473020-50473140Exon10: 35 residues, 50473613-50473713Exon11: 38 residues, 50475471-50475581Exon12: 55 residues, 50475672-50475832Exon13: 74 residues, 50482544-50482762Exon14: 36 residues, 50489446-50489550Exon15: 95 residues, 50492773-50493052Exon16: 28 residues, 50493240-50493320Exon17: 17 residues, 50494908-50494953Exon18: 972 residues, 50497471-50500381Exon19: 2 residues, -Jump to MARK4_HUMAN  
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Loci Cluster (Details)Loci: 3116 50100878-50104489 ~-4K 19057(APOE)(+)Loci: 3117 50234137-50266053 ~-32K 19065(SFRS16)(+)Loci: 4398 50407718-50429309 ~-22K 19076(-)Loci: 3118 50446389-50500381 ~-54K 19078(MARK4)(+)Loci: 4399 50546685-50565669 ~-19K 19089(ERCC2)(-)Loci: 4400 50747641-50779917 ~-32K 19109(OPA3)(-)Loci: 4401 50804499-50834509 ~-30K 19111(EML2)(-)Loci: 3119 50863341-50877557 ~-14K 19113(GIPR)(+)Loci: 4402 51134630-51168497 ~-34K 19134(NOVA2)(-)Loci: 3120 51542133-51585943 ~-44K 19149(PPP5C)(+)Loci: 3121 51796351-51805878 ~-10K 19157(CALM1)(+)Loci: 4403 51869413-51911506 ~-42K 19161(PRKD2)(-)Loci: 4404 52033262-52046043 ~-13K 19167(AP2S1)(-)Loci: 3115 50004177-50016517 ~-12K 19053(LU)(+)Link out to UCSC