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01433B_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
Description14-3-3 protein beta/alpha (protein kinase c inhibitor protein 1) (kcip-1) (protein 1054).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005515 protein binding (IPI)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The 14-3-3 proteins are a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimeric within all eukaryotic cells. There is a high degree of sequence identity and conservation between all the 14-3-3 isotypes.articularly in the regions which form the dimer interface or line the central ligand binding channel of the dimeric molecule. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus.he conserved core region and a divergent carboxyl terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain. cradle for interacting with client proteins. The monomer consists of nine helices organized in an antiparallel manner.orming an L-shaped structure. The interior of the L-structure is composed of four helices: H3 and H5.hich contain many charged and polar amino acids.nd H7 and H9.hich contain hydrophobic amino acids. These four helices form the concave amphipathic groove that interacts with target peptides. 14-3-3 proteins mainly bind proteins containing phosphothreonine or phosphoserine motifs however exceptions to this rule do exist. Extensive investigation of the 14-3-3 binding site of the mammalian serine/threonine kinase Raf-1 has produced a consensus sequence for 14-3-3-binding.SxpSxP (in the single-letter amino-acid x denotes any amino acid and p indicates that the next residue is phosphorylated). 14-3-3 proteins appear to effect intracellular signalling in one of three ways - by direct regulation of the catalytic activity of the bound protein.y regulating interactions between the bound protein and other molecules in the cell by sequestration or modification or by controlling the subcellular localisation of the bound ligand.Proteins appear to initially bind to a single dominant site and then subsequently to many.uch weaker secondary interaction sites. The 14-3-3 dimer is capable of changing the conformation of its bound ligand whilst itself undergoing minimal structural alteration.
  IPR000308:14-3-3 protein
SequencesProtein: 1433B_HUMAN (245 aa)
mRNA: NM_003404
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
The directed movement of substances, either within a vesicle or in the vesicle membrane, into, out of or within a cell.
sdb:0057 axon transport  (Evidence:keywords)
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
KO assignmentK06630
  Level 3 annotation:
    tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein
  Level 2 annotation:
    Cell cycle
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 62 residues, 42947757-42947941Exon2: 33 residues, 42949702-42949797Exon3: 103 residues, 42963585-42963888Exon4: 43 residues, 42966047-42966171Exon5: 56 residues, 42967022-42967186Exon6: 34 residues, 42968055-42968151Exon7: 714 residues, 42968436-42970574Exon8: 2 residues, -Jump to 1433B_HUMAN  
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Loci Cluster (Details)Loci: 3258 42947757-42970574 ~-23K 23159(YWHAB)(+)Loci: 3259 43028533-43142005 ~-113K 23166(STK4)(+)Loci: 4524 43154364-43163167 ~-9K 23170(KCNS1)(-)Loci: 3260 43478191-43488296 ~-10K 23191(PIGT)(+)Loci: 4523 42813862-42872326 ~-58K 23158(RIMS4)(-)Link out to UCSC