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Protein Page:
RKIP (human)

Overview
RKIP a metastasis suppressor that regulates extracellular matrix remodeling and tumor survival. Binds to and inhibits Raf-1. Phosphorylation by classic and atypical but not novel PKC isoforms dissociates this complex, relieving inhibition of the Raf/MAP kinase signaling cascade. Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation. Cleaved into hippocampal cholinergic neurostimulating peptide (HCMP) that appears to be involved in the function of the presynaptic cholinergic neurons of the central nervous system. HCNP increases the production of choline acetyltransferase but not acetylcholinesterase. Expressed in brain. Increased expression in aged senescence-accelerated mice. Note: This description may include information from UniProtKB.
Protein type: Lipid-binding; Protein kinase, regulatory subunit
Chromosomal Location of Human Ortholog: 12q24.23
Cellular Component: cytosol; nucleus
Molecular Function: enzyme binding; phosphatidylethanolamine binding; protein binding; protein kinase binding
Biological Process: MAPKKK cascade
Reference #:  P30086 (UniProtKB)
Alt. Names/Synonyms: HCNP; HCNPpp; Hippocampal cholinergic neurostimulating peptide; Neuropolypeptide h3; PBP; PEBP; PEBP-1; PEBP1; phosphatidylethanolamine binding protein 1; Phosphatidylethanolamine-binding protein 1; prostatic binding protein; Prostatic-binding protein; Raf kinase inhibitor protein; Raf kinase inhibitory protein; RKIP
Gene Symbols: PEBP1
Molecular weight: 21,057 Da
Basal Isoelectric point: 7.01  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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RKIP

Protein Structure Not Found.
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