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0RAF1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionRaf proto-oncogene serine/threonine-protein kinase (ec (raf- 1) (c-raf) (craf).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005741 mitochondrial outer membrane (TAS)
0005515 protein binding (IPI)
0004672 protein kinase activity (TAS)
0006915 apoptosis (TAS)
0008283 cell proliferation (TAS)
0006468 protein amino acid phosphorylation (TAS)
0007165 signal transduction (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:
This is the Ras-binding domain found in proteins related to Ras. It is foundin association with the PE-bind and pkinase domains.
  IPR003116:Raf-like Ras-binding
Diacylglycerol (DAG) is an important second messenger. Phorbol esters (PE) are analogues of DAG and potent tumor promoters that cause a variety of physiological changes when administered to both cells and tissues. DAG activates a family of serine/threonine protein kinases.ollectively known as protein kinase C (PKC) . Phorbol esters can directly stimulate PKC. The N-terminal region of PKC.nown as been shown to bind PE and DAG in a phospholipid and zinc-dependent fashion. The C1 region contains one or two copies (depending on the isozyme of PKC) of a cysteine-rich domain.hich is about 50 amino-acid residues long.nd which is essential for DAG/PE-binding. The DAG/PE-binding domain binds two zinc ions; the ligands of these metal ions are probably the six cysteines and two histidines that are conserved in this domain.
  IPR002219:Protein kinase C, phorbol ester/diacylglycerol binding
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
SequencesProtein: RAF1_HUMAN (648 aa)
mRNA: NM_002880
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
A process that increases short-term neuronal synaptic plasticity, the ability of neuronal synapses to change in the short-term as circumstances require. Short-term neuronal synaptic plasticity generally involves increasing or decreasing synaptic sensitivity.
sdb:0043 positive regulation of short-term neuronal synaptic plasticity  (Evidence:keywords)
the plasma membrane of the postsynaptic neuron. It apposes with presynaptic actiove zone.
sdb:0108 postsynaptic plasma membrane  (Evidence:keywords)
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
sdb:0265 cAMP mediated STP  (Evidence:keywords)
KO assignmentK04366
  Level 3 annotation:
    v-raf murine leukemia viral oncogene homolog 1
  Level 2 annotation:
    MAPK signaling pathway
    Insulin signaling pathway
    Regulation of actin cytoskeleton
    Focal adhesion
    Gap junction
    Natural killer cell mediated cytotoxicity
    Fc epsilon RI signaling pathway
    Long-term potentiation
    Long-term depression
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 350 residues, 12600107-12601156Exon2: 47 residues, 12601345-12601480Exon3: 46 residues, 12601620-12601752Exon4: 41 residues, 12602179-12602298Exon5: 17 residues, 12604089-12604136Exon6: 61 residues, 12607296-12607473Exon7: 30 residues, 12608206-12608291Exon8: 41 residues, 12616189-12616307Exon9: 44 residues, 12616650-12616778Exon10: 11 residues, 12616886-12616914Exon11: 53 residues, 12620634-12620788Exon12: 35 residues, 12622699-12622798Exon13: 54 residues, 12625264-12625422Exon14: 36 residues, 12625731-12625834Exon15: 39 residues, 12628448-12628561Exon16: 79 residues, 12635013-12635246Exon17: 124 residues, 12680311-12680678Exon18: 2 residues, -Jump to RAF1_HUMAN  
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