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Literature summary for 2.7.1.127 extracted from

  • Ashour, D.J.; Pelka, B.; Jaaks, P.; Wundenberg, T.; Blechner, C.; Zobiak, B.; Failla, A.V.; Windhorst, S.
    The catalytic domain of inositol-1,4,5-trisphosphate 3-kinase-a contributes to ITPKA-induced modulation of F-actin (2015), Cytoskeleton (Hoboken), 72, 93-100.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information generation of isozyme ITPKA mutant DELTA1-54 or DELTA1-134. Insertion of the enzyme's catalytic domain inbetween actin filaments increases its inositol-1,4,5-trisphosphate 3-kinase-a activity Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + 1D-myo-inositol 1,4,5-trisphosphate Homo sapiens
-
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P23677 gene Itpka
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 1D-myo-inositol 1,4,5-trisphosphate
-
Homo sapiens ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
?

Subunits

Subunits Comment Organism
More the N-terminus harbors the actin binding domain, the C-terminus of ITPKA acts as spacer between actin filaments Homo sapiens

Synonyms

Synonyms Comment Organism
inositol-1,4,5-trisphosphate 3-kinase-A
-
Homo sapiens
InsP3Kinase
-
Homo sapiens
ITPKA
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
Homo sapiens

General Information

General Information Comment Organism
physiological function isozyme ITPKA induces formation of complex actin networks, but exibits only one N-terminal actin binding domain, the C-terminus of ITPKA acts as spacer between actin filaments, overview. ITPKA induces the formation of a dense network of branched actin filaments, not of linear filaments. Overexpression of ITPKA induces the formation of lamellipodia-like protrusions which consist of cross-linked actin filaments. 1D-myo-inositol 1,3,4,5-tetrakisphosphate inhibits actin polymerization, but does not show a significant effect on bundling activity of ITPKA, while binding of ITPKA to actin stimulates inositol-1,4,5-trisphosphate 3-kinase-a activity Homo sapiens