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1Q15523_HUMAN*   Trembl (?) | Description Local Annotation Link Reference
General Information
NameN/A
DescriptionSerine/threonine protein kinase.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005634 nucleus (IEA)
0005524 ATP binding (IEA)
0000166 nucleotide binding (IEA)
0004674 protein serine/threonine kinase activity (IEA)
0016740 transferase activity (IEA)
0006468 protein amino acid phosphorylation (IEA)

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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
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:-92.8239087409443 
Location:152-411IPR000961:S_TK_X 
Evalue:-17.4202164033832 
Location:412-476
SequencesProtein: Q15523_HUMAN (479 aa)
mRNA: X80229
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
KO assignmentK06071
  Level 3 annotation:
    protein kinase N
  Level 2 annotation:
    Signal transduction mechanisms
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 26 residues, 14430110-14430187Exon2: 27 residues, 14435478-14435554Exon3: 49 residues, 14435639-14435781Exon4: 33 residues, 14435871-14435965Exon5: 27 residues, 14439376-14439453Exon6: 27 residues, 14439529-14439605Exon7: 32 residues, 14439687-14439779Exon8: 61 residues, 14441152-14441329Exon9: 23 residues, 14441563-14441626Exon10: 27 residues, 14441723-14441800Exon11: 49 residues, 14441974-14442117Exon12: 38 residues, 14442386-14442494Exon13: 29 residues, 14442582-14442663Exon14: 94 residues, 14443392-14443670Exon15: 2 residues, -Jump to Q15523_HUMAN  
Loci Cluster (Details)Loci: 4372 14380630-14391171 ~-11K 18171(DDX39)(-)Loci: 3093 14430110-14443670 ~-14K 18178(+)Loci: 4373 14852137-14853264 ~-1K 18201(-)Loci: 4374 14921990-14944730 ~-23K 18203(SLC1A6)(-)Loci: 4375 15325340-15351603 ~-26K 18217(AKAP8)(-)Loci: 4376 15351858-15390833 ~-39K 18218(AKAP8L)(-)Loci: 3094 15699833-15700862 ~-1K 18230(OR10H2)(+)Loci: 4377 15778890-15779847 ~-1K 18231(OR10H1)(-)Loci: 3095 16083489-16105443 ~-22K 18238(RAB8A)(+)Loci: 3096 16169730-16207156 ~-37K 18242(AP1M1)(+)Loci: 4378 16333407-16443762 ~-110K 18245(EPS15L1)(-)Loci: 4371 14119550-14177997 ~-58K 18165(LPHN1)(-)Link out to UCSC