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0MARK1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameMARK1
DescriptionSerine/threonine-protein kinase mark1 (ec 2.7.1.37) (map/microtubule affinity-regulating kinase 1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005737 cytoplasm (ISS)
0005856 cytoskeleton (ISS)
0005524 ATP binding (IDA)
0000287 magnesium ion binding (IDA)
0004674 protein serine/threonine kinase activity (IDA)
0007010 cytoskeleton organization and biogenesis (ISS)
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:
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:-107.244125144327 
Location:60-311IPR001772:KA1 
Evalue:-25 
Location:746-795IPR000449:UBA 
Evalue:-7.67778070526608 
Location:332-369
SequencesProtein: MARK1_HUMAN (795 aa)
mRNA: AF154845 NM_018650
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: 217 residues, 218768190-218768838Exon2: 70 residues, 218819318-218819522Exon3: 20 residues, 218821029-218821083Exon4: 18 residues, 218838295-218838344Exon5: 25 residues, 218844031-218844102Exon6: 21 residues, 218855903-218855960Exon7: 81 residues, 218858274-218858511Exon8: 42 residues, 218858600-218858720Exon9: 35 residues, 218870999-218871099Exon10: 39 residues, 218872165-218872278Exon11: 53 residues, 218875340-218875494Exon12: 66 residues, 218875797-218875991Exon13: 35 residues, 218890584-218890685Exon14: 57 residues, 218891950-218892115Exon15: 86 residues, 218893065-218893317Exon16: 708 residues, 218901776-218903895Exon17: 2 residues, -Jump to MARK1_HUMANExon1: 106 residues, 218768521-218768838Exon2: 70 residues, 218819318-218819522Exon3: 20 residues, 218821029-218821083Exon4: 18 residues, 218838295-218838344Exon5: 24 residues, 218839762-218839828Exon6: 25 residues, 218844031-218844102Exon7: 21 residues, 218855903-218855960Exon8: 81 residues, 218858274-218858511Exon9: 42 residues, 218858600-218858720Exon10: 35 residues, 218870999-218871099Exon11: 39 residues, 218872165-218872278Exon12: 53 residues, 218875340-218875494Exon13: 66 residues, 218875797-218875991Exon14: 35 residues, 218890584-218890685Exon15: 57 residues, 218891950-218892115Exon16: 86 residues, 218893065-218893317Exon17: 17 residues, 218897754-218897799Exon18: 217 residues, 218901776-218902423Exon19: 2 residues, -Jump to MARK1_HUMAN  
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Loci Cluster (Details)Loci: 2593 218930284-218939116 ~-9K 3962(+)Loci: 2592 218768190-218903895 ~-136K 3959(MARK1)(+)Link out to UCSC