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0SN1L2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSNF1LK2
DescriptionSerine/threonine-protein kinase snf1-like kinase 2 (ec 2.7.1.37) (qin- induced kinase).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005737 cytoplasm (ISS)
0005524 ATP binding (IDA)
0000287 magnesium ion binding (IDA)
0004674 protein serine/threonine kinase activity (IDA)
0006468 protein amino acid phosphorylation (IDA)
0007243 protein kinase cascade (IDA)
0046626 regulation of insulin receptor signaling pa... (ISS)

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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 entry includes protein kinases from eukaryotes and viruses and may include some bacterial hits too.
  IPR000719:Protein kinase
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
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:-100.958607314842 
Location:20-271IPR011009:Kinase_like 
Evalue:0 
Location:772-841IPR000449:UBA 
Evalue:0 
Location:295-335IPR001245:TYRKINASE 
Evalue:0 
Location:0-0
SequencesProtein: SN1L2_HUMAN (926 aa)
mRNA: NM_015191
Local Annotation
Synapse Ontology
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 85 residues, 110978379-110978632Exon2: 41 residues, 110992176-110992293Exon3: 23 residues, 110996272-110996336Exon4: 56 residues, 111063934-111064096Exon5: 43 residues, 111076819-111076944Exon6: 43 residues, 111077385-111077509Exon7: 75 residues, 111079136-111079357Exon8: 53 residues, 111080920-111081073Exon9: 57 residues, 111088144-111088309Exon10: 78 residues, 111095708-111095937Exon11: 97 residues, 111096411-111096696Exon12: 56 residues, 111096832-111096996Exon13: 39 residues, 111097763-111097874Exon14: 32 residues, 111098598-111098690Exon15: 1139 residues, 111099429-111102840Exon16: 2 residues, -Jump to SN1L2_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3990 111102849-111142313 ~-39K 7727(PPP2R1B)(-)Loci: 2704 111462831-111471727 ~-9K 7743(SDHD)(+)Loci: 2705 111602308-111609903 ~-8K 7753(PTS)(+)Loci: 2703 110978379-111102840 ~-124K 7726(SNF1LK2)(+)Link out to UCSC