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0TNIK_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameTNIK
DescriptionTraf2 and nck interacting kinase (ec 2.7.1.37).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005524 ATP binding (NAS)
0004674 protein serine/threonine kinase activity (IDA)
0007254 JNK cascade (TAS)
0006468 protein amino acid phosphorylation (NAS)
0007243 protein kinase cascade (IDA)
0006445 regulation of translation (IDA)
0006950 response to stress (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:
Based on sequence similarities a domain of homology has been identified in the following proteins :Citron and Citron kinase. These two proteins interact with the GTP-bound forms of the small GTPases Rho and Rac but not with Cdc42.Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCKalpha). This serine/threonine kinase interacts with the GTP-bound form of the small GTPase Cdc42 and to a lesser extent with that of Rac.NCK Interacting Kinase (NIK). serine/threonine protein kinase.ROM-1 and ROM-2.rom yeast. These proteins are GDP/GTP exchange proteins (GEPs) for the small GTP binding protein Rho1.This domain.alled the citron homology domain.s often found after cysteine rich and pleckstrin homology (PH) domains at the C-terminal end of the proteins . It acts as a regulatory domain and could be involved in macromolecular interactions .
  IPR001180:Citron-like
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 () 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
IPR001180:CNH 
Evalue:-116.721246399047 
Location:1042-1340IPR002290:S_TKc 
Evalue:-95.9208187539524 
Location:25-289
SequencesProtein: TNIK_HUMAN (1360 aa)
mRNA: AB011123
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: 488 residues, 172262985-172264447Exon2: 48 residues, 172266669-172266809Exon3: 55 residues, 172267058-172267218Exon4: 52 residues, 172269330-172269480Exon5: 35 residues, 172271705-172271806Exon6: 47 residues, 172280000-172280135Exon7: 50 residues, 172282733-172282877Exon8: 59 residues, 172284637-172284808Exon9: 39 residues, 172285600-172285712Exon10: 57 residues, 172287824-172287989Exon11: 45 residues, 172294321-172294451Exon12: 63 residues, 172301931-172302116Exon13: 10 residues, 172307665-172307689Exon14: 34 residues, 172308547-172308645Exon15: 56 residues, 172311196-172311360Exon16: 37 residues, 172324078-172324185Exon17: 82 residues, 172326394-172326634Exon18: 57 residues, 172329196-172329361Exon19: 65 residues, 172338673-172338862Exon20: 31 residues, 172339952-172340039Exon21: 39 residues, 172340881-172340992Exon22: 70 residues, 172357942-172358147Exon23: 24 residues, 172361752-172361819Exon24: 60 residues, 172367577-172367753Exon25: 28 residues, 172375734-172375813Exon26: 20 residues, 172377808-172377863Exon27: 45 residues, 172389184-172389315Exon28: 32 residues, 172391179-172391270Exon29: 39 residues, 172395007-172395118Exon30: 44 residues, 172411598-172411724Exon31: 21 residues, 172428647-172428704Exon32: 24 residues, 172570102-172570168Exon33: 109 residues, 172660489-172660812Exon34: 2 residues, -Jump to TNIK_HUMAN  
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