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Literature summary for 2.7.1.158 extracted from

  • Poehlmann, J.; Fleig, U.
    Asp1, a conserved 1/3 inositol polyphosphate kinase, regulates the dimorphic switch in Schizosaccharomyces pombe (2010), Mol. Cell. Biol., 30, 4535-4547.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
D333A kinase dead mutant of Asp1 Schizosaccharomyces pombe
H397A phosphatase dead mutant of Asp1 Schizosaccharomyces pombe

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Schizosaccharomyces pombe 5737
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
143000
-
Asp1-Pk1-green fluorescent protein, gel filtration Schizosaccharomyces pombe

Organism

Organism UniProt Comment Textmining
Schizosaccharomyces pombe
-
-
-

Synonyms

Synonyms Comment Organism
ASP1
-
Schizosaccharomyces pombe
inositol polyphosphate kinase
-
Schizosaccharomyces pombe

General Information

General Information Comment Organism
malfunction a functional Asp1 kinase domain abolishes invasive growth which is monopolar Schizosaccharomyces pombe
physiological function Asp1 kinase activity regulates cell-cell adhesion and increases resistance towards thiabendazole. The Asp1 kinase activity encoded by the N-terminal part of the protein is regulated negatively by the C-terminal domain of Asp1. Asp1 is a key regulator of the morphological switch via the cAMP protein kinase A Schizosaccharomyces pombe