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0LATS2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameLATS2
DescriptionSerine/threonine-protein kinase lats2 (ec 2.7.1.37) (large tumor suppressor homolog 2) (serine/threonine-protein kinase kpm) (kinase phosphorylated during mitosis protein) (warts-like kinase).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005634 nucleus (NAS)
0000922 spindle pole (IDA)
0005524 ATP binding (IDA)
0004674 protein serine/threonine kinase activity (IDA)
0000082 G1/S transition of mitotic cell cycle (IDA)
0009755 hormone-mediated signaling (IDA)
0045736 negative regulation of cyclin dependent pro... (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:
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
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
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 signalling via protein kinases . HHR23A.he human homologue of yeast Rad23A is a nucleotide excision-repair protein that contains both an internal and a C-terminal UBA domain. The fold of the UBA domain consists of a compact three-helical bundle with a right-handed twist.nd have a conserved hydrophobic surface patch for protein-protein interactions. UBA-like domains can be found in other proteins as well.uch as the TS-N domain in the elongation factor Ts (EF-Ts).hich catalyses the recycling of the GTPase EF-Tu required for the binding of aminoacyl-tRNA top the ribosomal A site ; and the C-terminal domain of TAP/NXF1.hich functions in nuclear export through the interaction of its UBA-like domain with FG nucleoporins .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR009060:UBA-like
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:-95.1487416512809 
Location:668-973IPR000961:Pkinase_C 
Evalue:-6.92081880569458 
Location:992-1046IPR000449:UBA 
Evalue:-3.35654735565186 
Location:99-139
SequencesProtein: LATS2_HUMAN (1088 aa)
mRNA: NM_014572
Local Annotation
Synapse Ontology
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: 309 residues, 20446578-20447503Exon2: 37 residues, 20451829-20451936Exon3: 63 residues, 20453604-20453787Exon4: 196 residues, 20455362-20455945Exon5: 476 residues, 20460019-20461443Exon6: 46 residues, 20463410-20463543Exon7: 184 residues, 20517823-20518369Exon8: 58 residues, 20533484-20533654Exon9: 2 residues, -Jump to LATS2_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2806 20648371-20651218 ~-3K 10108(+)Loci: 4090 20446578-20533654 ~-87K 10104(LATS2)(-)Link out to UCSC