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Literature summary for 3.4.21.105 extracted from

  • Pascall, J.C.; Brown, K.D.
    Intramembrane cleavage of ephrinB3 by the human rhomboid family protease, RHBDL2 (2004), Biochem. Biophys. Res. Commun., 317, 244-252.
    View publication on PubMed
Search for more literature for 3.4.21.105

Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ephrin B3 + H2O Homo sapiens RHBDL-2 mediated proteolytic processing may regulate intercellular interactions between ephrinB3 and eph receptors ?
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 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ephrin B3 + H2O RHBDL-2 mediated proteolytic processing may regulate intercellular interactions between ephrinB3 and eph receptors Homo sapiens ?
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 ?
ephrin B3 + H2O cleaved efficiently, appears to be cleaved in its membrane domain Homo sapiens ?
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 ?
additional information membrane domains of several mammalian EGF-faily proteins are not cleaved by RHBDL2, suggesting that the endogenous targets of the human protease are not EGF-related factors. Amino acid sequence at the luminal face of the membrane domain of a substrate protein determines whether it is cleaved by RHBDL2 Homo sapiens ?
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 ?
protein Spitz + H2O UniProt Accession Code QRHBDL2 cleaves the membrane domain of Drosophila protein Spitz, when the proteins are coexpressed in mammalian cells Homo sapiens ?
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 ?

Synonyms

Synonyms Comment Organism
RHBDL2
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 Homo sapiens