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0SGK2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSGK2
DescriptionSerine/threonine-protein kinase sgk2 (ec 2.7.1.37) (serum/glucocorticoid regulated kinase 2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0015459 potassium channel regulator activity (IDA)
0004682 protein kinase CK2 activity (NAS)
0004674 protein serine/threonine kinase activity (TAS)
0017080 sodium channel regulator activity (NAS)
0006468 protein amino acid phosphorylation (NAS)
0007243 protein kinase cascade (TAS)
0006979 response to oxidative stress (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
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:-101.36653154442 
Location:95-352IPR000961:S_TK_X 
Evalue:-14.7695510786217 
Location:353-419
SequencesProtein: SGK2_HUMAN (427 aa)
mRNA: NM_016276
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
Na channel plays an important role in the course of action potential.
sdb:0287 Na channel  (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: 146 residues, 41628150-41628585Exon2: 18 residues, 41629121-41629171Exon3: 21 residues, 41629718-41629776Exon4: 30 residues, 41629969-41630053Exon5: 46 residues, 41631438-41631570Exon6: 39 residues, 41632670-41632783Exon7: 14 residues, 41633077-41633114Exon8: 31 residues, 41634104-41634191Exon9: 34 residues, 41636962-41637058Exon10: 54 residues, 41638277-41638433Exon11: 32 residues, 41642025-41642115Exon12: 262 residues, 41646905-41647686Exon13: 2 residues, -Jump to SGK2_HUMAN  
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