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Literature summary for 3.4.24.B28 extracted from

  • Kleino, I.; Ortiz, R.M.; Yritys, M.; Huovila, A.P.; Saksela, K.
    Alternative splicing of ADAM15 regulates its interactions with cellular SH3 proteins (2009), J. Cell. Biochem., 108, 877-885.
    View publication on PubMed
Search for more literature for 3.4.24.B28

Cloned(Commentary)

Cloned (Comment) Organism
expressed as a GST-fusion protein in Escherichia coli Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens in contrast other ADAM15 isoforms ADAM15i3 interacts preferentially with Hck and Lyn containing proteins ?
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 ?
nephrocystin + H2O Homo sapiens strong co-precipitation of nephrocystin from cell lysates is specific to ADAM15 isoforms i4, i5, and i6 ?
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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.
additional information in contrast other ADAM15 isoforms ADAM15i3 interacts preferentially with Hck and Lyn containing proteins Homo sapiens ?
-
 ?
nephrocystin + H2O strong co-precipitation of nephrocystin from cell lysates is specific to ADAM15 isoforms i4, i5, and i6 Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
ADAM15 endopeptidase recommended name Homo sapiens
ADAM15 isoforms i1 different isoforms exist due to alternative mRNA splicing. Isoform i1 does not contain clusters of proline residues Homo sapiens
ADAM15 isoforms i2 different isoforms exist due to alternative mRNA splicing Homo sapiens
ADAM15 isoforms i3 different isoforms exist due to alternative mRNA splicing. Isoform i3 contains a single unique proline cluster not found in other ADAM15 isoforms Homo sapiens
ADAM15 isoforms i4 different isoforms exist due to alternative mRNA splicing Homo sapiens
ADAM15 isoforms i5 different isoforms exist due to alternative mRNA splicing Homo sapiens
ADAM15 isoforms i6 different isoforms exist due to alternative mRNA splicing Homo sapiens

General Information

General Information Comment Organism
physiological function alternative mRNA splicing generates several ADAM15 isoforms containing different combinations of putative Src homology-3 (SH3) domain binding sites in their cytosolic tails. Alternative use of ADAM15 exons profoundly influences selection of SH3-containing cellular partner proteins, including the avid interactions with nephrocystin and sorting nexin-33 Homo sapiens