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FLASH GENE
Symbol PEBP1 contributors: mct/npt/pgu - updated : 20-06-2014
HGNC name phosphatidylethanolamine binding protein 1
HGNC id 8630
Location 12q24.23      Physical location : 118.573.869 - 118.583.390
Synonym name
  • prostatic binding protein
  • Raf kinase inhibitor protein
  • hippocampal cholinergic neurostimulating peptide
  • prostatic binding protein
  • neuropolypeptide h3
  • Synonym symbol(s) RKIP, HCNP, PEBP, PBP, HCNPpp, PEBP-1
    DNA
    TYPE functioning gene
    STRUCTURE 9.52 kb     4 Exon(s)
    MAPPING cloned Y linked N status confirmed
    RNA
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    4 - 1507 21 187 - 2008 18294816
    EXPRESSION
    Type ubiquitous
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Endocrineadrenal gland   highly
     parathyroid   highly
     thyroid   highly
    Hearing/Equilibriumear   highly
    Reproductivefemale systemplacenta  highly Homo sapiens
    Visualeyeretina    Homo sapiens
    cells
    SystemCellPubmedSpeciesStageRna symbol
    Visualcone photoreceptor Homo sapiens
    Visualrod photoreceptor Homo sapiens
    cell lineage
    cell lines
    fluid/secretion
    at STAGE
    PROTEIN
    PHYSICAL PROPERTIES
    STRUCTURE
    motifs/domains
    HOMOLOGY
    interspecies homolog to murine Pbp1
    Homologene
    FAMILY
  • phosphatidylethanolamine-binding protein family
  • CATEGORY regulatory
    SUBCELLULAR LOCALIZATION extracellular
        intracellular
    intracellular,cytoplasm,organelle,mitochondria,outer
    intracellular,cytoplasm,organelle,membrane
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    intracellular,cytoplasm,organelle,Golgi
    basic FUNCTION
  • protein kinase inhibitor protein that regulates the activity of the Raf/MEK/ERK module
  • inhibits the phosphorylation and activation of MEK by RAF1
  • may be involved in the function of the presynaptic cholinergic neurons of the central nervous system
  • increases the production of choline acetyltransferase
  • negative modulator of the Raf-MEK-ERK signaling pathway
  • conserved pocket may constitute a novel phosphoamino-acid binding motif and is absolutely required for PEBP1 function
  • novel component of the SNAI1 transcriptional regulatory network important for the progression and metastasis of cancer
  • negatively regulates the MAP kinase (MAPK), G protein-coupled receptor kinase-2, and NF-kappaB signalling cascades
  • modulates cell cycle kinetics and motility
  • physiologic inhibitor of RAF1 kinase and nuclear factor kappaB signaling that represses tumor invasion and metastasis
  • prevents cilia formation and is associated with CEP290-mediated photoreceptor degeneration
  • potentially modulates the localization of a distinct set of proteins required for cilia assembly and maintenance
  • its ability to interact with RAB8A suggests its involvement in the regulation of docking and transport of membrane protein-containing vesicles in photoreceptors
  • regulates growth and differentiation signaling of mitogen-activated protein kinases (MAPK), GRK2 and NF-kappaB pathways each of which regulates cytotrophoblast differentiation and normal placental development
  • novel factor expressed in cytotrophoblast cells where it likely regulates cell migration
  • positive feedback loop between PEBP1 and TBK1 that is essential for type I interferon production in anti-viral innate immunity
  • CELLULAR PROCESS cell life, cell death/apoptosis
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling signal transduction
    a component
    INTERACTION
    DNA
    RNA
    small molecule nucleotide, other,
  • ATP binding
  • opioids
  • phosphatodylethanolamine
  • protein
  • interacting with RAF1 (binds to RAF1 interfering with binding of the MEK substrate and potentially also RAF1 activation))
  • negatively correlated with the expression of SNAI1 zinc-transcriptional repressor, a key modulator of normal and neoplastic epithelial-mesenchymal transition (EMT) program
  • binds GSK3 proteins and maintains GSK3B protein levels and its active form
  • binds to RAF1 kinase and inhibits the RAS-RAF1-MEK1/2- ERK1/2 pathway
  • interacting with RAB8A (interacts preferably with the GDP-bound form of RAB8A in the retina)
  • inhibits breast tumour metastasis in part via MIRLET7A1
  • RAF1 and ADRBK1 are direct interaction partners of PEBP1 (PEBP1 dimer formation controls its target switch from RAF1 to ADRBK1)
  • inhibits syndecan-2 (SDC2), which is aberrantly expressed in breast cancer, via downregulation of HMGA2
  • PEBP1 is essential for TBK1 activation and type I interferon production triggered by viral infection
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional     --low  
    its inhibition results in increased cell proliferation by affecting spindle checkpoint, resulting in chromosomal aberrations and cancer progression
    constitutional     --over  
    in CEP290-associated photoreceptor degeneration
    constitutional     --low  
    increased the level of free RAF1 and thereby elevated the mitochondrial translocation of RAF1 during HBx-mediated hepatocarcinogenesis
    tumoral     --low  
    associated to poor prognosis in hepatocellular carcinoma related to hepatitis B infection
    constitutional     --low  
    might be responsible for dementia associated with high-altitude hypoxia
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    SystemTypeDisorderPubmed
    cancer  
    PEBP1/GSK3 axis is both a potential therapeutic target and a prognosis-based predictor of cancer progression
    cancer  
    key metastasis suppressor and potential therapeutic agent
    ANIMAL & CELL MODELS
  • Pebp1 deficiency renders the mice more susceptible to vesicular stomatitis virus (VSV) and herpes simplex virus (HSV) infections